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lexA

Gene
lexA
Protein
LexA repressor
Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
Length
275 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
29.575 kDa
Sequence
MKRSTPRPARSQAALTTSSEESPDRVERGGDGVATVTDFPDGPPDETGLTPRQRRILDVIRDSVRRRGYPPSMREIGEAVGLTSTSSVAHQLMVLQRKGFLRRDPNRPRAVEIRSAESAVPDASAGHSPAADRAPSARRPPRGPSPIDSNPDVVAVPLVGRIAAGGPALAEQLIEDVVPLPRQLVGEGTLFLLQVKGDSMVDAAICDGDWVVVRQQPVAENGDIVAAMIDGEATVKTFKRRGAHIWLMPHNPQYEPIPGDEATILGRVVAVLRRL

Gene
lexA
Protein
LexA repressor
Organism
Corynebacterium jeikeium (strain K411)
Length
267 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
29.006 kDa
Sequence
MSIDESSDNPTPRPKLGRPPKSEADKRAEKEAQKDGKKPALSTRQRRILEVIRDSTIIRGYPPSIREIADAVGLHSTSSVSYHLTQLEKRGYLRRDGKRPRAVDVRAFDGGQLTNESTKKNAGSPQPTSAAIPEPTTEGETMPEATYVPVVGQIAAGAPILAEQNVEAHFPLPQELVGNGELFLLQVVGESMHDAGIFNGDWVVVRSQSVAEFGDFVAAMIDGEATVKEFQKDADGLWLIPHNPLFEPIPAEEATILGKVAAVLRKI

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
Length
257 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
28.169 kDa
Sequence
MFDFIGVSRYASKELRKEPIVSTIPFTPKKSDERPDESTLTDRQRKVLDAIKTHLAKQGFAPSFREIGEAAGLKSPSSVKHQLQVLDEKGFIRMNANKGRAIEVVNLNDEEPNGKVAQVIPFPSQDDACGSIMASHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGTGNLFMLEVHGDSMIDAAICDGDFVVVREQNSAENGDIVAALLDDEATVKTFRKDHGHVWLIPHNPAYSPIDGTHAEIMGKVVTVLRKI

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
Length
257 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
28.169 kDa
Sequence
MFDFIGVSRYASKELRKEPIVSTIPFTPKKSDERPDESTLTDRQRKVLDAIKTHLAKQGFAPSFREIGEAAGLKSPSSVKHQLQVLDEKGFIRMNANKGRAIEVVNLNDEEPNGKVAQVIPFPSQDDACGSIMASHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGTGNLFMLEVHGDSMIDAAICDGDFVVVREQNSAENGDIVAALLDDEATVKTFRKDHGHVWLIPHNPAYSPIDGTHAEIMGKVVTVLRKI

Gene
lexA
Protein
LexA repressor
Organism
Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3)
Length
256 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
27.302 kDa
Sequence
MTSQGRGTRRGGTRGNVRAFPEGPTDAGLTPRQRRVLEVIRAAVERRGYPPSVREIGEAVGLTSTSSVAHQLKVLEEKGYLRRDPNRPRAMEVLTVEHPRQRADVGAGATTVAGTIPIVGEAAPGTTEGSKSDAAYVPVLGRIAAGGPILAEQAVEDVFPLPREIVGEGTLFLLRVVGDSMINAAICDGDWVVVRQQPVADNGEIVAAMIDGEATVKRLRVRDGKIWLHPENSAFADIPGEDATILGRIVAVLRRV

Gene
lexA
Protein
LexA repressor
Organism
Frankia alni (strain ACN14a)
Length
253 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.918 kDa
Sequence
MTSQGRGTRRGGARGNVRAFPENPADAAGLTPRQRKVLEVIRAEVERRGYPPSVREIGEAVGLTSTSSVAHQLKVLEEKGYLRRDPNRPRAMEVLSPDRPRRKADSGAAAVVSTFPGAAAAPAGVGGEGSAAYVPVLGRIAAGGPILAEQAIEDVFPLPKEIVGEGTLFLLRVVGESMINAAICDGDWVVVRQQPVADNGEIVAAMIDGEATVKRLRVRDGKIWLHPENPTFSDIPGEEATILGRIVAVLRRI

Gene
lexA
Protein
LexA repressor
Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Length
253 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
27.763 kDa
Sequence
MLTRKQHELLLFIDRHLKQTGFSPSFDEMKDALNLRSKSGIHRLISALEERDFLRRRHHRARALEVLRLPETMPAATGKPPLAESGPPPVTAPATDESAAAESFVPNVIKGDFANRLAGASVATEAGAIHLPFYGRIAAGQPIEALRETGAQIEVPMNLLGHGEHYALEVAGDSMIEAGILDGDTVIIRRGDVAQNGQIVVALIDDQEVTLKRLRRRGSTIALEPANARYEPRIVPSDRVRIQGQLVGLLRRY

Gene
lexA
Protein
LexA repressor
Organism
Corynebacterium glutamicum (strain R)
Length
253 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
27.272 kDa
Sequence
MAIEKKPAGARGSRGSRTVKTLPNGKPDPASLSDRQRRILEVIRDAVVLRGYPPSIREIGDAAGLQSTSSVAYQLKELEKKGFLRRDPNKPRAVDVRHLPETESRSSKAATQAKSKAPQAGAHDPELAGQTSFVPVVGKIAAGSPITAEQNIEEYYPLPAEIVGDGDLFMLQVVGESMRDAGILTGDWVVVRSQPVAEQGEFVAAMIDGEATVKEFHKDSSGIWLLPHNDTFAPIPAENAEIMGKVVSVMRKL

Gene
lexA
Protein
LexA repressor
Organism
Thermobifida fusca (strain YX)
Length
252 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
27.434 kDa
Sequence
MPEENRGGHQPYTEESSVSALHPVRTDDSVGSSAEQTGDAPTLTERQRSVLNVIHRYVRERGYPPSIREIGEAVGLSSPSSVAHQLKVLQRKGYLHRDQNRPRAVEIRIPHKTSGRTRRELGGLSGSEEIVDIPLLGRIAAGGPILAEEHVEDVLSLPRQLVGEGTLFMLTVVGDSMIDAAIADGDLVVVRQQPDANNGDIVAALLGDEATVKVFKRDREHVWLLPRNSAYDPINGDSATILGKVVTVLRKV

Gene
lexA
Protein
LexA repressor
Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Length
251 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
27.25 kDa
Sequence
MLTRKQYLLLSFIDQRLKLSGVSPSFDEMKDALGLKSKSGIHRLIKGLEERGFLKRLPHRARALEVLRLPCNLTFDGDGEALDDGQPAPLFGGPLPETGFSPQVIRGNFTPTLPSTQVPQVLFTESISLPLLGKIAAGTPIAALIDPTSSIDVPASMVRGGEHFALRIEGDSMIEAGILSGDLAVVRRCDEAENGTVIVALVDNEEATLKRLRRKGASIALEPANRAFKTQIYGPDRVRIQGRLVGLIRSY

Gene
lexA
Protein
LexA repressor
Organism
Frankia sp. (strain EAN1pec)
Length
250 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.601 kDa
Sequence
MTSQERGTRRGDTRGNVRDFPDSPADASGLTQRQKKVLEVIRSAVERRGYPPSVREIGEAVGLTSTSSVAHQLKVLQEKGFLRRDPNRPRAMEVLPIGGAKTGGRSRAGAAAAAGAPAETTALEAGTPTYVPLVGRIAAGGPILAEQAIEDVYPLPKEIVGEGTLFLLKVVGQSMINAAICDGDFVVVRQQPVADNGEIVAAMIDGEATVKRFRQRDGRVWLAPENPAFSDIPAEDATILGRIVAVMRRV

Gene
lexA
Protein
LexA repressor
Organism
Arthrobacter sp. (strain FB24)
Length
249 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.884 kDa
Sequence
MAAQATGGRATQRSQQSPAKPKGLTVRQKKILETIQRSVNDNGYPPSMREIGDTVGLASLSSVTHQLSQLEKLGYLRRDPKRPRAMEVLMPLTLDEGTAKISGVEKPARLRTIGGLAVSELATATDTAMVPLVGRIAAGGPILADQVVEDVMPLPRQLVGHGELFMLKVTGDSMIDAAICDGDWVVVRRQSDAVNGDIVAALLDDEATVKTFRQRDGHTWLLPQNTQYEPILGDHANIMGKVVSVFRSL

Gene
lexA
Protein
LexA repressor
Organism
Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6)
Length
249 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.379 kDa
Sequence
MAAAATGGRATSQPKKTTKGLTPRQKKILETIQRSVNVNGYPPSMREIGDTVGLASLSSVTHQLSQLEKLGYLRRDPKRPRAMEVLMPLTLDGGATGRTARQAAEPAAAAAPGITASVTELPTALDTAMVPLVGRIAAGGPILADQVVEDVMPLPRQLVGQGELFMLKVAGDSMVDAAICDGDWVVVRRQADAANGDIVAALLDDEATVKTFRQRDGHTWLLPQNTQYEPILGDHATIMGKVVSVLRSL

Gene
lexA
Protein
LexA repressor
Organism
Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6)
Length
249 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.379 kDa
Sequence
MAAAATGGRATSQPKKTTKGLTPRQKKILETIQRSVNVNGYPPSMREIGDTVGLASLSSVTHQLSQLEKLGYLRRDPKRPRAMEVLMPLTLDGGATGRTARQAAEPAAAAAPGITASVTELPTALDTAMVPLVGRIAAGGPILADQVVEDVMPLPRQLVGQGELFMLKVAGDSMVDAAICDGDWVVVRRQADAANGDIVAALLDDEATVKTFRQRDGHTWLLPQNTQYEPILGDHATIMGKVVSVLRSL

Gene
lexA
Protein
LexA repressor
Organism
Paenarthrobacter aurescens (strain TC1)
Length
247 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.322 kDa
Sequence
MAAKATGGGAPLRSQQPQKSPKSLTVRQKKILETIQRSVNDNGYPPSMREIGDTVGLASLSSVTHQLSQLEKLGYLRRDPKRPRAMEVLMPLTLDGGAIPGVEAPTTLRSAGGLAVTELASASDTAMVPLVGRIAAGGPILADQTVEDVLALPRQLVGHGELFMLKVAGDSMIDAAICDGDWVVVRRQNDAINGDIVAALLDDEATVKTFRQRDGHTWLLPQNTQYEPILGDQATIMGKVVSVLRSL

Gene
lexA
Protein
LexA repressor
Organism
Nocardioides sp. (strain ATCC BAA-499 / JS614)
Length
246 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.607 kDa
Sequence
MATPQTGKKTPSRRVSELPDGPPDATGLTPRQQRVLAHIKDSIEKRGYPPSMREIGEAVGLTSSSSVAHQLKTLEEKGFLKRDPHRPRALEVFLPEVMAARRSMSAAEESSFDETGVGDALPAAQYVPVVGRIAAGGPILAEERVEDVFPLPRQLVGDGQLFLLEVRGDSMIEAAICDGDYVAIRQQPTAENGEIVAAMIDGEATVKTFQRKDGNVWLLPHNPAYDPIDGTHATILGKVTAVLRRV

Gene
lexA
Protein
LexA repressor
Organism
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Length
245 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.496 kDa
Sequence
MLTRKQHELLMFIHERLKESGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLNAAKKFSPSVIQGSLGQGGLGRQIKPAPSRLPAAGNDDDAVSAVSIPVMGRIAAGVPIDAIQHQTHSISVPPDMIMGGEHYALEVKGDSMIDAGIFDGDTVIIRNADTASPGEIVVALVDEEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Length
244 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.736 kDa
Sequence
MSDSSDTTVDGASDGASDGASGADNRAQLVDTALTERQRTILNVIRTSVNDRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGADDTVTAAPVTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGQGTLFLLKVVGESMIEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQIWLMPHNPAFDPIPGNDATVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium ulcerans (strain Agy99)
Length
244 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.722 kDa
Sequence
MSDSSDTTVDGASDGASDGASGADNRAQLVDTALTERQRTILNVIRTSVNDRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGADDTVTAAPVTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGQGTLFLLKVVGESMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQIWLMPHNPAFDPIPGNDATVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Length
243 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.778 kDa
Sequence
MSDDTGEFTDGSTESPADADGAGRRRAVDNGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRAADDPAAAAVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRARGQVWLMPHNPAYDPIPGNEAAVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)
Length
242 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.647 kDa
Sequence
MLTRKQYELLLLIDGHLRKTGFSPSFEEMKAALNLKSKSGIHRLISALEERGFLRRRHHRARALEVIRMPEAASMPVPKTAPSAPSFASPPAFTPNVIQGSFSSRIAGVRAAQDASAVQLPLYGRIAAGMPIEALRDTSAYLSVPIDMLGNGEHYALEVAGDSMIDAGIFDGDTVIIQQSDLAENGQIVVALIDDTEVTLKRLRRRGKSVALEPANERHETRIFPADRVRVQGRLIGLLRRY

Gene
lexA
Protein
LexA repressor
Organism
Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1)
Length
242 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.519 kDa
Sequence
MLTRKQLDLLRFIQSRMQECGVPPSFDEMKDALDLKSKSGIHRLITALEERGFLRRLPNRARAIEVIRIPESLTQAAPAPQTPAEPRRFTPSVVEGGKSKQPPAPASTRMIDESGRAISIPVMGRIAAGTPVSAIQNQSHAITLSPDFVAGGEHYALEVRGDSMVEAGILDGDLVVIRKQDTANTGDIIVALIDDEEATLKRLRRRGSSIALEAANPAYETRVLGPDRVRIQGRLVSLVRRY

Gene
lexA
Protein
LexA repressor
Organism
Ruegeria sp. (strain TM1040)
Length
241 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.705 kDa
Sequence
MLTKKQLQLLEFIHKRLQKDGVPPSFDEMKTALDLRSKSGIHRLITALEERGFIRRLAHRARAIEVIRLPDSLGGGGALGAASDGFQPKVIAGGRGDSADGGAAAELKPVADTGATELTIMGRIAAGVPIEAINQAAAHVAVPNAMLSSSGQHYALEVRGDSMIDAGINDGDVVVIRETDAADNGDIVVALVEGHEATLKRFERKGRMIELHAANPAYPTRSYTEDQVKVQGRLVGLIRTY

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium longum (strain DJO10A)
Length
241 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.049 kDa
Sequence
MSTIPFSPKQKPDESTLTDRQRKVLDAIRTHIDEQGFAPSFREIGNAAGLKSPSSVKHQLQVLEDKGFIRMNANKGRAIEVVAGSAPNAEKPSQASEEATSTSNVAEIYQFPAEAIAESHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGSGTLFMLEVHGDSMVDAAICDGDYVVVREQNSAVNGDIVAALLDDEATVKTFRKENGHVWLMPHNPAYSPIDGTHATIMGKVVTVLRKL

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium longum (strain NCC 2705)
Length
241 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.049 kDa
Sequence
MSTIPFSPKQKPDESTLTDRQRKVLDAIRTHIDEQGFAPSFREIGNAAGLKSPSSVKHQLQVLEDKGFIRMNANKGRAIEVVAGSAPNAEKPSQASEEATSTSNVAEIYQFPAEAIAESHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGSGTLFMLEVHGDSMVDAAICDGDYVVVREQNSAVNGDIVAALLDDEATVKTFRKENGHVWLMPHNPAYSPIDGTHATIMGKVVTVLRKL

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Length
241 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.075 kDa
Sequence
MSTIPFSPKQKPDESTLTDRQRKVLDAIRTHIDEQGFAPSFREIGNAAGLKSPSSVKHQLQVLEDKGFIRMNANKGRAIEVVAGSAPNPEKPSQASEEATSTSNVAEIYQFPAEAIAESHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGSGTLFMLEVHGDSMVDAAICDGDYVVVREQNSAVNGDIVAALLDDEATVKTFRKENGHVWLMPHNPAYSPIDGTHATIMGKVVTVLRKL

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium longum (strain DJO10A)
Length
241 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.049 kDa
Sequence
MSTIPFSPKQKPDESTLTDRQRKVLDAIRTHIDEQGFAPSFREIGNAAGLKSPSSVKHQLQVLEDKGFIRMNANKGRAIEVVAGSAPNAEKPSQASEEATSTSNVAEIYQFPAEAIAESHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGSGTLFMLEVHGDSMVDAAICDGDYVVVREQNSAVNGDIVAALLDDEATVKTFRKENGHVWLMPHNPAYSPIDGTHATIMGKVVTVLRKL

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium longum (strain NCC 2705)
Length
241 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.049 kDa
Sequence
MSTIPFSPKQKPDESTLTDRQRKVLDAIRTHIDEQGFAPSFREIGNAAGLKSPSSVKHQLQVLEDKGFIRMNANKGRAIEVVAGSAPNAEKPSQASEEATSTSNVAEIYQFPAEAIAESHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGSGTLFMLEVHGDSMVDAAICDGDYVVVREQNSAVNGDIVAALLDDEATVKTFRKENGHVWLMPHNPAYSPIDGTHATIMGKVVTVLRKL

Gene
lexA
Protein
LexA repressor
Organism
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Length
241 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.075 kDa
Sequence
MSTIPFSPKQKPDESTLTDRQRKVLDAIRTHIDEQGFAPSFREIGNAAGLKSPSSVKHQLQVLEDKGFIRMNANKGRAIEVVAGSAPNPEKPSQASEEATSTSNVAEIYQFPAEAIAESHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGSGTLFMLEVHGDSMVDAAICDGDYVVVREQNSAVNGDIVAALLDDEATVKTFRKENGHVWLMPHNPAYSPIDGTHATIMGKVVTVLRKL

Gene
lexA
Protein
LexA repressor
Organism
Brucella abortus (strain S19)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella abortus (strain S19)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.13 kDa
Sequence
MLTRKQLDLLRFIQQRMRETGVPPSFDEMKDALDLKSKSGIHRLITALEERGFLRRLPNRARAIEVIRIPDAVVPPSGEVVRFTPSVVEGGRTAAPAAKAAPMPSSLGSDDNGRSISIPVMGRIAAGTPISAIQSQSRTVAMSPDFLAGGEHYALEVRGDSMIEAGILDGDLVVIRRQDTANTGDIVVALIDDEEATLKRLRRRGSSIALEAANPAYETRVLGPDRVRIQGRLVSLIRKY

Gene
lexA
Protein
LexA repressor
Organism
Brucella abortus (strain 2308)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella abortus biovar 1 (strain 9-941)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella canis (strain ATCC 23365 / NCTC 10854)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella melitensis biotype 2 (strain ATCC 23457)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.084 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTIIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella suis (strain ATCC 23445 / NCTC 10510)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Brucella suis biovar 1 (strain 1330)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.07 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLSPQKKFAPSVIEGSLGKVASVQPVRPAPAPQNSEAPATVSVPVMGRIAAGVPISAIQNQTHMLSLPPEMIGAGEHYALEVKGDSMIDAGIFDGDTVIIKRGDTANPGEIVVALVDEEEATLKRFRREGASIALEAANPAYETRIFGPDRVHVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Agrobacterium fabrum (strain C58 / ATCC 33970)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.033 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYTPGARPQRGFSPSVIEGSLGKPKEPEPAPAVKAPANDFAGAATIPVMGRIAAGVPISAIQNNTHDLAVPVDMLGSGEHYALEVKGDSMIEAGIFDGDTVIIRNGNTANPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKIQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Agrobacterium radiobacter (strain K84 / ATCC BAA-868)
Length
240 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.147 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYSPSLQPRRGFSPSVIEGSLGKPQPVQPPAPAKPANDENNSAVSVPVMGRIAAGVPISAIQNNTHDITVPADMLGSGEHYALEVKGDSMIDAGIFDGDTVIIRNSTTANPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.681 kDa
Sequence
MTEAATGPEGADPSRAARSLPGRPPGIRADSSGLTDRQRRVIEVIRDSVQRRGYPPSMREIGQAVGLSSTSSVAHQLMALERKGFLRRDPHRPRAYEVRGSDQPSAQPADTSGKPAASYVPLVGRIAAGGPILAEESVEDVFPLPRQLVGDGELFVLKVVGDSMIEAAICDGDWVTVRRQPVAENGDIVAAMLDGEATVKRFKRENGHVWLLPHNAAYQPIPGDDATILGKVVAVLRRV

Gene
lexA
Protein
LexA repressor
Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.92 kDa
Sequence
MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLNAQKKFAPSVIEGSLGKTPPPPARPAPVATNDDTSGTVSVPVMGRIAAGVPISAIQNQTHSLSLPPEMIGAGEHYALEVRGDSMIDAGIFDGDTVIIKRGDSANPGEIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVRVQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Methylobacterium sp. (strain 4-46)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.021 kDa
Sequence
MLTRKQLDLLRFIQQRMRETGVPPSFDEMKDALDLKSKSGIHRLITALEERGFLRRLPNRARAIEVIRIPEAVASGPAEVVRFTPSVVEGGRSSAPVKPAPLPTALVSDESGHAVSIPVMGRIAAGTPISAIQSQSRSVAMSPDFLAGGEHYALEVRGDSMIEAGILDGDLVVIRRQDTANTGDIVVALIDDEEATLKRLRRRGSSIALEAANPAYETRVLGPDRVRIQGRLVSLIRKY

Gene
lexA
Protein
LexA repressor
Organism
Rhizobium etli (strain CIAT 652)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.764 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYSPSLQPRRGFSPSVIEGSLGKPPAVAAPAAAKPIADNGNSVSVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEHYALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhizobium etli (strain CFN 42 / ATCC 51251)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.874 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYNPSLQPRRGFSPSVIEGSLGKPQPVAAPAAPKPVADNGNSISVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEHYALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhizobium leguminosarum bv. viciae (strain 3841)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.853 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYSPSIQPRRGFSPSVIEGSLGKPQPVATPAPAKSVADNGNSVSVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEHYALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhizobium leguminosarum bv. trifolii (strain WSM2304)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.805 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYSPSIQPRRGFSPSVIEGSLGKPQPAAAPAPAKPVADNGNSVSVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEHYALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhizobium radiobacter
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.622 kDa
Sequence
MLTRKQQELLLFIHGTNEGNPGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYAGASQVRRGFSPTVIEGSLGKLASPPPAPKPAPPAEAASVAVPVMGRIAAGVPISAIQNNMHDISVPVEMIGSGEHYALEIKGDSMIEAGILDGDTVIIRNGSTASPGDIVVALIDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKIQGRLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Agrobacterium vitis (strain S4 / ATCC BAA-846)
Length
239 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.181 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAMTSSIPPRRTGFSPSVIEGSRGKLQAVPSAPAKQVEEVRNSSSIPVMGRIAAGVPISAIQNNTHDISVPMEMLGSGEHYALEVKGDSMIEAGILDGDTVIIRNATTANPGDIVVALVDDEEATLKRFRRRGASIALEAANPAYETRIFGPDRVKIQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Gluconobacter oxydans (strain 621H)
Length
238 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.47 kDa
Sequence
MLTRKQHQLLLYIDDHLRRTGYSPSFDEMKDALELRSKSGIHRLISALEERGFLRRHHHRARALEVLRLPHMGTEAPAATGTGTAFVPAVLNQGQTGLEGAFSEASVANDRQTVSIPLYGRIAAGLPIEAMQDDSDRIDVPVSLLGTGEHYALTVAGDSMIEAGILDGDIAIIRRRETAENGQIIVALIDEQEVTLKKLRRRGSMIALEAANRDYETRIFPAERVHIQGRLVALFRQY

Gene
lexA
Protein
LexA repressor
Organism
Sinorhizobium medicae (strain WSM419)
Length
238 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.781 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYAGNPQVRRGFSPSVIEGSLGKPAAPAPAPKPAPPAENASVVVPVMGRIAAGVPISAIQNNMHDISVPIEMIGSGEHYALEIKGDSMIEAGILDGDTVIIRNASTASIGDIVVALIDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKIQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhizobium meliloti (strain 1021)
Length
238 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.667 kDa
Sequence
MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYAGASQVRRGFSPSVIEGSLGKPAAPPPAPKPAPPAEAASVAVPVMGRIAAGVPISAIQNNMHDISVPVEMIGSGEHYALEIKGDSMIEAGILDGDTVIIRNGSTASPGDIVVALIDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKIQGRLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhodobacter capsulatus
Length
238 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.106 kDa
Sequence
MLTHKQLELLDFIQKRMARDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRMAHRARALEIVKLPESMERAAEAERGLQTQPAFTPMLIAGSRTEPPRGALPVAAAALDIPMMGRIAAGVPIEAIAEVAHHVTVPGAMLSGRGEHYALEVKGDSMIQAGINDGDIVVIRSQPTAENGDIVVALVEDLEATLKRYYRRGGMIALEAANPAYETRLLREDQVKVQGRLVGLIRSY

Gene
lexA
Protein
LexA repressor
Organism
Bartonella quintana (strain Toulouse)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.908 kDa
Sequence
MLTCKQYELLLFIHNHMKEIGVPPSFDEMKIALELTSKSGIHRLITALEERGFIRRLPNRARAVEVVRLPEKITFNLSSARKISPNVIENNRRKISKNSKNLNNFDIEDKKNVTVPIMGRIAAGVPVSAIQQQTNTLCLPADMISLGEHYALEVKDDSMIEAGILDKDTIIVRRQNTATPGEIIIALIDKEEATLKRYRRNGASIALEAANPHYETRIYRPERIEIQGKLIGLIRKY

Gene
lexA
Protein
LexA repressor
Organism
Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.392 kDa
Sequence
MLTKKQSELLRFIHERLKETGVPPSFDEMKEALDLRSKSGIHRLVMALEERGFIRRLPNRARALEVVRLPDAATPPVPPHGRKFSPSVIEGDLGRVRPHTPHTDDEDSELTTVAIPVMGRIAAGTPISALQHRSHTIGLPMDMLPAGEHYALEVRGDSMIDAGILDADTVIIRRQDNAENGDIVVALIDDEEATLKRLRRRGASIALEPANSAYETRIFGPDRVRIQGKLVSLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Bartonella quintana (strain Toulouse)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.908 kDa
Sequence
MLTCKQYELLLFIHNHMKEIGVPPSFDEMKIALELTSKSGIHRLITALEERGFIRRLPNRARAVEVVRLPEKITFNLSSARKISPNVIENNRRKISKNSKNLNNFDIEDKKNVTVPIMGRIAAGVPVSAIQQQTNTLCLPADMISLGEHYALEVKDDSMIEAGILDKDTIIVRRQNTATPGEIIIALIDKEEATLKRYRRNGASIALEAANPHYETRIYRPERIEIQGKLIGLIRKY

Gene
lexA
Protein
LexA repressor
Organism
Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.392 kDa
Sequence
MLTKKQSELLRFIHERLKETGVPPSFDEMKEALDLRSKSGIHRLVMALEERGFIRRLPNRARALEVVRLPDAATPPVPPHGRKFSPSVIEGDLGRVRPHTPHTDDEDSELTTVAIPVMGRIAAGTPISALQHRSHTIGLPMDMLPAGEHYALEVRGDSMIDAGILDADTVIIRRQDNAENGDIVVALIDDEEATLKRLRRRGASIALEPANSAYETRIFGPDRVRIQGKLVSLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.762 kDa
Sequence
MLTRKQHELLMFIHERIKEGGVSPSFDEMKEALDLRSKSGIHRLITALEERGFIRRLPHRARALEILKLPDAASPSLAMARGRGFSPSVIEGGAQPKPSSRDLAPARSSGDTMTLSVMGRIAAGTPIEALQEESHQVSVPLNLLGSGEHYALEVKGDSMIEAGILDGDTVLIQRCDTATSGDIVVALVDGYEATLKRLRKKGDSIALEAANPAYETRIFGPDRVKVQGKLVGLLRRY

Gene
lexA
Protein
LexA repressor
Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.707 kDa
Sequence
MPVKDSSSNKKNQIGKLSERQRRILEVITDAVSLRGYPPSIREIGDAAGLQSTSSVAYQLKELEKKGYLRRDPNKPRAVDVRALPDPIPSKPGRKPGPKKSSVAISPDPAETSPTSFVPIVGSIAAGNPILAEENVDGYFPFPSEIVGDGDLFMLQVEGESMRDAGILHHDWVVVRSQPVAEQGEFVAALIEGEATVKEFHSDSSGVWLLPHNDAFDPIPAEHAEIMGKVVSILRKL

Gene
lexA
Protein
LexA repressor
Organism
Rhodospirillum centenum (strain ATCC 51521 / SW)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.111 kDa
Sequence
MLTRKQQELLLFIHERLKDGGVSPSFDEMKDALGLKSKSGIHRLITGLEERGFIRRLPHRARALEVLRLPEQPAPLRVAPRTEEPVRFRPNVIRGDFRGALPGREARGDAEAVSLPLYGRIAAGLPIEALRDTTASIDVPTGLIASGEHYALEVAGDSMVDAGILDGDTVIIQRCETAENGTVIVALVDDNEVTLKRLRRKGNSIALEPANPAYETRVFGADRVRIQGRLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Rhodopseudomonas palustris (strain BisA53)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.196 kDa
Sequence
MLTRKQFELLRFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPEFGINGGGQTRRGFTPSVIEGHLGKVRPHASIGSDEDSHDRNVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGSGEHYALEVRGDSMVDAGILDGDMALIQKNESADTGDIVVALIDEEEATLKRFRRRGASIALEPANSAYEVRILPPNRVRIQGKLVGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Rhodopseudomonas palustris (strain BisB18)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.88 kDa
Sequence
MLTRKQYELLRFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELGVNPGGGNGRRGFTPSVIEGNLGRVRPAASLGGDDDSGRTVAVPVMGRIAAGTPIEALQTRSHTISMPADMLGSGEHYALEVRGDSMVDAGILDGDMALIQKNDSADTGDIVVALIDEEEATLKRFRRRGASIALEPANAAYEVRILPPNRVRIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Length
237 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.887 kDa
Sequence
MLTRKQYDLLRFIHERLKETGVPPSFDEMKEALDLRSKSGIHRLITALEERGFIRRLPNRARALEVVRLPDSVAPGLATPRSASRGFSPSVIEGSLGKVRPAADDDEGAGQVVTVPVMGRIAAGSPISAIQTRSHTLNIPPEMLGSGEHFALEVRGDSMIEAGILDGDTVLIRKCDTADTGDIIVALVDDEEATLKRLRKKGASIALEAANPAYETRIFGPDRVRIQGRLIGLMRRY

Gene
lexA
Protein
LexA repressor
Organism
Chelativorans sp. (strain BNC1)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.703 kDa
Sequence
MLTRKQHELLLFIHARLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLAAPRKFSPSVIEGGQGRSSPAPRPAANNDDETSVVSIPVMGRIAAGVPIDAIQHRTHSIGVPPDMITGGEHYALEVKGDSMIEAGIFDGDTVIIRQTQAANPGDIVVALVDEEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGRLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.74 kDa
Sequence
MLTRKQYDLLRFIHERLKETGVPPSFDEMKEALDLRSKSGIHRLITALEERGFIRRLPNRARALEVVRLPDSAAPGLAAARSGGRGFSPSVIEGSLGRVRPVVDDEEPAAVVAVPVMGRIAAGSPISAIQTRSNTLNLPPEMLGTGEHFALEVRGDSMIEAGILDGDTVLIRKCDTADTGDIIVALVDDEEATLKRLRRKGASIALEAANPAYETRIFGPDRVRIQGRLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Rhodopseudomonas palustris (strain TIE-1)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.912 kDa
Sequence
MLTRKQFELLKFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPDTGGMPGNSRRGFTPSVIEGNLGKVRPPSPTPAEDDHDRGSVAVPVMGRIAAGTPIEALQSRSHTISVPADMLGSGEHYALEVRGDSMVEAGILDGDMALIQKNDVADTGDIVVALIDEEEATLKRFRRRGASIALEPANAAYEVRILPPNRVRIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.129 kDa
Sequence
MLTKKQSELLRFINERMKETGVPPSFDEMKDALDLRSKSGIHRLIIALEERGFIRRLPNRARALEVLRMPGASAADAGRGRKFEPSVIEGHLGRVRPMPAARDDEDGARAMVAIPVMGRIAAGTPISALQTRSHTLNLPPEMLSQGEHYALEVRGDSMIDAGIFDADTVLIRKQDTAETGDIVVALIDDEEATLKRLRRRGASIALEAANPAYETRIFGPDRVRIQGKLVGLIRRY

Gene
lexA
Protein
LexA repressor
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.912 kDa
Sequence
MLTRKQFELLKFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPDTGGMPGNSRRGFTPSVIEGNLGKVRPPSPTPAEDDHDRGSVAVPVMGRIAAGTPIEALQSRSHTISVPADMLGSGEHYALEVRGDSMVEAGILDGDMALIQKNDVADTGDIVVALIDEEEATLKRFRRRGASIALEPANAAYEVRILPPNRVRIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.813 kDa
Sequence
MNDSNDTSVAGGAAGADSRVLSADSALTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGADDAALPPVTEVAGSDALPEPTFAPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGTLFLLKVIGDSMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.813 kDa
Sequence
MNDSNDTSVAGGAAGADSRVLSADSALTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGADDAALPPVTEVAGSDALPEPTFAPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGTLFLLKVIGDSMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.813 kDa
Sequence
MNDSNDTSVAGGAAGADSRVLSADSALTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGADDAALPPVTEVAGSDALPEPTFAPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGTLFLLKVIGDSMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.841 kDa
Sequence
MNDSNDTSVAGGAAGADSRVLSADSALTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGADDAALPPVTEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGTLFLLKVIGDSMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response).
Similarity
Belongs to the peptidase S24 family.
Mass
24.841 kDa
Sequence
MNDSNDTSVAGGAAGADSRVLSADSALTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGADDAALPPVTEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGTLFLLKVIGDSMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
236 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Has been shown to bind to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.841 kDa
Sequence
MNDSNDTSVAGGAAGADSRVLSADSALTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGADDAALPPVTEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGTLFLLKVIGDSMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Caulobacter sp. (strain K31)
Length
235 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.65 kDa
Sequence
MLTRKQHELLMFIHERIKESGVSPSFDEMKEALDLASKSGIHRLITALEERGFIRRLAHRARALEVVKLPQQATTAAPPKGRGAFRPQVLEGGGQAPTTSAQPQMAADNSRELPILGRIAAGTPIDAIQHERERLPVPESMLGAGEHYVLEVQGDSMIEAGILDGDYVIIKKGDTANSGEIVVALVGEEATLKRLRKKGGSIALEAANPKYETRIFGPDQVEVQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhodopseudomonas palustris (strain BisB5)
Length
235 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.895 kDa
Sequence
MLTRKQFELLKFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPDLGGNTGGGRRGFTPSVIEGTLGKVRPPSHSHAEDESDRNVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGSGEHYALEVRGDSMVEAGILDGDMALIQRNESAETGDIVVALIDEEEATLKRFRRRGASIALEPANAAYEVRILPPNRVRIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Length
235 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.467 kDa
Sequence
MLTRKQYELLMFIDERLRATGISPSFDEMKDALDLKSKSGIHRLITGLEERGFIRRLAHRARALEVVRLPENRNDQTLPPPAKAFAPNVIKGGFAASQLAGAPVAGPSDSVTLPLYGKIAAGTPIEALRDHSNSVDIPASMLGSGNHYALTVDGDSMIEAGINDGDTVVIRSCDSAETGTIVVALVDDTEVTLKRLRRKGTSVALEPANKAYETRVLPPDRVKVQGRLVGLLRRY

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium leprae (strain Br4923)
Length
235 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.089 kDa
Sequence
MSDSTDISGITVDGRLHSMDSGLTERQRTILNVIRASVTSRGYPPSIREIADAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGVEETQAAGPAVLTEVAGSDVLPEPTFVPILGRIAAGSPIFAEGTVEDIFPLPRELVGEGTLFLLKVTGDSMVEAAICDGDWVVVRQQKVADNGDIVAAMIDGEATVKTFKRAGGQVWLIPHNPAFDPIPGNDATVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium leprae (strain TN)
Length
235 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.089 kDa
Sequence
MSDSTDISGITVDGRLHSMDSGLTERQRTILNVIRASVTSRGYPPSIREIADAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGVEETQAAGPAVLTEVAGSDVLPEPTFVPILGRIAAGSPIFAEGTVEDIFPLPRELVGEGTLFLLKVTGDSMVEAAICDGDWVVVRQQKVADNGDIVAAMIDGEATVKTFKRAGGQVWLIPHNPAFDPIPGNDATVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.329 kDa
Sequence
MLTRKQHELLMFIHERIKETGVSPSFDEMKEALDLASKSGIHRLITALEERGFIRRLAHRARALEVVKLPQQATAAAPPKGRGAFRPQVFEGGGAPPPAASPAAAANDSRELPILGRIAAGTPIDAIQHERERLPVPEAMLGAGEHYVLEVQGDSMIEAGILDGDYVIIKKGDTATSGEIVVALVGEEATLKRLRKKGGSIALEAANPKYETRIFGPDQVEVQGKLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.776 kDa
Sequence
MLTCKQYELLLFIHNHMKETGVPPSFDEMKTALELTSKSGIHRLITALEERGFIRRLPNRARAVEVIRLPEKITFNLSSARKISPSVIENNKRKISKNSDNFDLEEKKNIIIPIMGRIAAAVPISAIQQQINTLCLPQDMISLGEHYALEVKDDSMIEAGILDKDIIIVRRQNTATSGEIIIALIDKEEVTFKRYRRKGNSITLEAANPHYETRIYRPERVQIQGKLIGLIRKY

Gene
lexA
Protein
LexA repressor
Organism
Polaromonas naphthalenivorans (strain CJ2)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.909 kDa
Sequence
MRTFNDFSGLPADRPKLTARQAQILELIRNAIAQTGAPPTRAEIAAELGFRSPNAAEEHLKALAKKGVIELVSGTSRGIRLRTDSLQALNESRISQFSPPVQRLEQLTLPLVGRVAAGSPILAQEHIERTYFFESRLFEQQPDYLLKVRGMSMRDIGIMDGDLLAVKQAREAKNGQIVVARLGDEVTVKRFHRNQHLIELLSENPDFKPIVVQPGEPFELEGLAVGLIRGSLAM

Gene
lexA
Protein
LexA repressor
Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.883 kDa
Sequence
MSILNDFSHLSSEGPKLTARQQQILELIQSAITRTGAPPTRAEIANELGFKSANAAEEHLQALARKGVIELVSGTSRGIRLRSDTLRSIHESRVKQFSLPLQSLAQLALPLVGRVAAGSPILAQEHIEQTYYFESSLFQRQPDYLLKVRGMSMRDAGIIDGDLLAVKQAKEARNGQIVVARIGDEVTVKRFRRTKHLIELLPENPDFKTIVVEPGEPFELEGLAVGLIRNTMLI

Gene
lexA
Protein
LexA repressor
Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
26.776 kDa
Sequence
MLTCKQYELLLFIHNHMKETGVPPSFDEMKTALELTSKSGIHRLITALEERGFIRRLPNRARAVEVIRLPEKITFNLSSARKISPSVIENNKRKISKNSDNFDLEEKKNIIIPIMGRIAAAVPISAIQQQINTLCLPQDMISLGEHYALEVKDDSMIEAGILDKDIIIVRRQNTATSGEIIIALIDKEEVTFKRYRRKGNSITLEAANPHYETRIYRPERVQIQGKLIGLIRKY

Gene
lexA
Protein
LexA repressor
Organism
Polaromonas naphthalenivorans (strain CJ2)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.909 kDa
Sequence
MRTFNDFSGLPADRPKLTARQAQILELIRNAIAQTGAPPTRAEIAAELGFRSPNAAEEHLKALAKKGVIELVSGTSRGIRLRTDSLQALNESRISQFSPPVQRLEQLTLPLVGRVAAGSPILAQEHIERTYFFESRLFEQQPDYLLKVRGMSMRDIGIMDGDLLAVKQAREAKNGQIVVARLGDEVTVKRFHRNQHLIELLSENPDFKPIVVQPGEPFELEGLAVGLIRGSLAM

Gene
lexA
Protein
LexA repressor
Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.883 kDa
Sequence
MSILNDFSHLSSEGPKLTARQQQILELIQSAITRTGAPPTRAEIANELGFKSANAAEEHLQALARKGVIELVSGTSRGIRLRSDTLRSIHESRVKQFSLPLQSLAQLALPLVGRVAAGSPILAQEHIEQTYYFESSLFQRQPDYLLKVRGMSMRDAGIIDGDLLAVKQAKEARNGQIVVARIGDEVTVKRFRRTKHLIELLPENPDFKTIVVEPGEPFELEGLAVGLIRNTMLI

Gene
lexA
Protein
LexA repressor
Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.4 kDa
Sequence
MNEATSHEGPKRSLPGRPPGIRADSSGLTDRQRRVIEVIRDSVQRRGYPPSMREIGQAVGLSSTSSVAHQLMALERKGFLRRDPHRPRAYEVRGSDQSSSVQPTDTAGKPAASYVPLVGRIAAGGPILAEESVEDVFPLPRQLVGDGELFVLKVVGDSMIEAAICDGDWVTVRRQPVAENGDIVAAMLDGEATVKRFKREDGHVWLLPHNSAYQPIPGDEATILGKVVAVLRRV

Gene
lexA
Protein
LexA repressor
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.311 kDa
Sequence
MSDAANPEGHKRSLPGRPPGIRADSSGLTDRQRRVIEVIRDSVQRRGYPPSMREIGQAVGLSSTSSVAHQLMALERKGFLRRDPHRPRAYEVRGSDQAASVQPTDTAGKPAASYVPLVGRIAAGGPILAEESVEDVFPLPRQLVGDGELFVLKVVGDSMIEAAICDGDWVTVRRQPVAENGDIVAAMLDGEATVKRFKREDGHVWLLPHNSAYEPIPGDDATILGKVVAVLRRV

Gene
lexA
Protein
LexA repressor
Organism
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.414 kDa
Sequence
MLTRKQHELLTFIQTRLEDSGISPSFEEMKEALDLKSKSGVHRLISALEERGFIRRLPNRARALEVLRQPDSAVGKAAPVSQREAANTNSALPPLRAAPKAAPAPANDVIELPLHGKIAAGVPIEALETTATLPVPAALLGAGEHYALEVSGDSMVEAGIFDGDYALVRKTDVARDGEIVVALVRGEEATLKYLHREKGMVRLDPANAAYDPQYYRPEEVAVQGKLAGLLRRYH

Gene
lexA
Protein
LexA repressor
Organism
Rhodopseudomonas palustris (strain HaA2)
Length
234 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.858 kDa
Sequence
MLTRKQFELLKFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPDLGGNSGARRGFTPSVIEGNLGKVRPPSPQHAEDDSDRNVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGSGEHYALEVRGDSMMDAGILDGDMALIQRNESADTGDIVVALIDEEEATLKRFRRRGASIALEPANSAYEVRILPPNRVRIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Roseobacter denitrificans (strain ATCC 33942 / OCh 114)
Length
233 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.052 kDa
Sequence
MLTKKQLDLLEFIHKRVQRDGVPPSFDEMKEALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPETLGGAARGGFTPRVIEGDKPDAPLPAGAQAVSSADAVALPLVGRIAAGLPIEAINQNSASVAVPGQMLSGKGDHYALEVKGDSMIDAGINDGDVVVIRETSVADNGDIVVALIEDHEATLKRYMRKGSSIALEAANPAYETRVFTEDKVKVQGKLVGLIRTY

Gene
lexA
Protein
LexA repressor
Organism
Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14)
Length
233 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.56 kDa
Sequence
MLTRKQYELLRFINERLKESGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPEVAGNGGGRRGFTPSVIEGNLGKVRPSGGGVVDDAERPVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGSGEHYALEVRGDSMVEAGILDGDMALIQRNETAETGDIVVALIDDEEATLKRFRRRGASIALEPANTAYEVRILPPNRVQIQGKLIGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255)
Length
233 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.403 kDa
Sequence
MLTRKQYELLRFINERLKESGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELAASGGGRRGFTPSVIEGNLGKVRRGGGGGADEAERPVAVPVMGRIAAGTPIEALQTCSHTISLPPDMLGAGEHYALEVRGDSMVDAGILDGDMALIQRNPTADTGDIVVALIDDEEATLKRFRRRGASIALEPANAAYEVRILPPNRVQIQGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Erythrobacter litoralis (strain HTCC2594)
Length
233 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.42 kDa
Sequence
MLTAKQHELIRFIQQRLEETGISPSFEEMKEALDLKSKSGVHRLISALEERGFIRRLPNRARALEILKQPEDVVGGGAKAAQSGSEASNVVDIRTAQAKTVPAPINDVVEIPLHGRIAAGAPIEALEDHQSLPVPAALLGPGDHYALEVSGDSMIEAGIFDGDFALIRRTDSARDGEIVVALVNNEEATLKYLHRDSGRVRLDPANASYEAQVYDPHQVQVQGKLAGLLRRYH

Gene
lexA
Protein
LexA repressor
Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.651 kDa
Sequence
MLTRKQYELLRFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELSQAASNRRGFTPSVIEGNLGKVRTSTPALDDGERPVAVPVMGRIAAGTPIEALQTRSHTISVPADMLGNGDHYALEVRGDSMVDAGILDGDMALIQRNETADTGDIVVALIDDEEATLKRFRRRGASIALEPANTAYEVRILPPNRVKIQGKLVGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Bradyrhizobium sp. (strain ORS 278)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.635 kDa
Sequence
MLTRKQYELLRFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELSQAAGNRRGFTPSVIEGNLGKVRTSTPALEDGERPVAVPVMGRIAAGTPIEALQTRSHTISVPADMLGNGDHYALEVRGDSMVDAGILDGDMALIQRNETADTGDIVVALIDDEEATLKRFRRRGASIALEPANTAYEVRILPPNRVKIQGKLVGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.651 kDa
Sequence
MLTRKQYELLRFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELSQAASNRRGFTPSVIEGNLGKVRTSTPALDDGERPVAVPVMGRIAAGTPIEALQTRSHTISVPADMLGNGDHYALEVRGDSMVDAGILDGDMALIQRNETADTGDIVVALIDDEEATLKRFRRRGASIALEPANTAYEVRILPPNRVKIQGKLVGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Bradyrhizobium sp. (strain ORS 278)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.635 kDa
Sequence
MLTRKQYELLRFINERLKEAGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELSQAAGNRRGFTPSVIEGNLGKVRTSTPALEDGERPVAVPVMGRIAAGTPIEALQTRSHTISVPADMLGNGDHYALEVRGDSMVDAGILDGDMALIQRNETADTGDIVVALIDDEEATLKRFRRRGASIALEPANTAYEVRILPPNRVKIQGKLVGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.51 kDa
Sequence
MLTRKQYELLRFINERLKESGIPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLANRARAIEVIKLPEPALGSGGRRGFTPSVIEGNLGKARGPASFDESGEQPVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGAGEHYALEVRGDSMVEAGILDGDMALIQRSENADTGDIVVALIDEEEATLKRFRRRGASIALEPANTAYEVRILPPNRVRIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Paracoccus denitrificans (strain Pd 1222)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.645 kDa
Sequence
MLTRKQIQLLEFIQARMARDGVPPSFDEMKLALDLRSKSGIHRLVTALEERGFIRRLPHRARALEIVRLPESLSKGPGFQPRVIEGTMPDRPAPLPRGAMEVSVSAIELPVMGRIAAGVPIEAISEISHHIAVPTTMLSGQDRHYALEVRGDSMIEAGINDGDVVVIREQNAAESGDIVVALVDGYEATLKRYRRKGNMIALEAANPAYETRVLPEDKVRIQGRLVGLIRSY

Gene
lexA
Protein
LexA repressor
Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.145 kDa
Sequence
MLPNGKPDPASLSDRQRRILEVIRDAVVLRGYPPSIREIGDAAGLQSTSSVAYQLKELEKKGFLRRDPNKPRAVDVRHLPETDNRTKAGPKAKARPTAGASPQPELASSTSFIPVVGKIAAGSPILAEQNIEEYYPLPADIVGDGELYMLQVVGESMRDAGILDGDWVVVRSQPVAEQGEFVAAMIEGEATVKEFHKDASGIWLLPHNDSFAPIPAENAEIMGKVVSVMRKL

Gene
lexA
Protein
LexA repressor
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.135 kDa
Sequence
MPNGKPDPASLSDRQRRILEVIRDAVVLRGYPPSIREIGDAAGLQSTSSVAYQLKELEKKGFLRRDPNKPRAVDVRHLPETESRSSKAATQAKSKAPQAGVHDPELAGQTSFVPVVGKIAAGSPITAEQNIEEYYPLPAEIVGDGDLFMLQVVGESMRDAGILTGDWVVVRSQPVAEQGEFVAAMIDGEATVKEFHKDSSGIWLLPHNDTFAPIPAENAEIMGKVVSVMRKL

Gene
lexA
Protein
LexA repressor
Organism
Maricaulis maris (strain MCS10)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.467 kDa
Sequence
MLTRKQNELLLFIHNRIKETGVSPSFDEMKGALQLASKSGVHRLITALEERGFIRRLAHRARALEVLKLPESAAAHETPAIPKGDLGANVVRGNFAKPEPDARENTVDIPMLGRIAAGVPISAIQHETDRFPVPADMVMGGEHFGLEVKGDSMIEAGIMDGDTVLIRRCQSAETGDIVVALIDDEEATLKRLRKKGGSVALEAANPEYETRIFPPDRVKVQGRLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium avium (strain 104)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.631 kDa
Sequence
MDDSNDSSSAGPDGRLHAVDPSLTERQRTILNVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGVDDDVAAPATEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGDGTLFLLKVVGDSMVEAAICDGDWVVVRQQHVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium gilvum (strain PYR-GCK)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.747 kDa
Sequence
MSDDSSDSTDAPGTSRSRDSGLTERQRTILDVIRASVTTRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDANRPRAVDVRAADDHPTPIVATEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGESMVDAAICDGDWVVVRQQSVADNGDIVAAMIDGEATVKTFKRTKGQVWLMPHNPAFDPIPGNDAAILGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.661 kDa
Sequence
MDDSNDSSSAGPDGRLHAVDPSLTERQRTILNVIRSSVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGVDDDVAAPATEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGDGTLFLLKVVGDSMVEAAICDGDWVVVRQQHVADNADIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1)
Length
232 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.579 kDa
Sequence
MSDDSSDSTSGAGSGRGRDSGLTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGSDDHAAPIVATDVAGSDSLPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGESMIDAAICDGDWVVVRQQSVADNGDIVAAMIDGEATVKTFKRTKGQVWLMPHNPAFDPIPGNDAAILGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Anaeromyxobacter sp. (strain Fw109-5)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.435 kDa
Sequence
MDALTDRQLEVLRFIARQIEDNGYPPTIREIGEALDIRSTNGVNDHLKALERKGFLTRDPVKSRALIPTPQAREVLGGGARASNVVPFTRTPAVGLKPAGRLVEIPILGRVAAGQPILAQERVEDTVQVDSFLLGTNKKVYGLRVQGDSMIGDGILPGDYIFVKKQLHAEDGDIVVAMIDEEATVKRVYFEGDRVRFQPSNPRMAPIYVRGSDFRTTMILGVVVGVYRKLG

Gene
lexA
Protein
LexA repressor
Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.219 kDa
Sequence
MLTKKQLDLLEFIHKRLQADGVPPSFDEMKLALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPESLGGEPTVGFQPRVIDGDRPDRPRPANAEPVTIHAVELPVMGRIAAGVPIEAISQVSHQVAVPGSMVGKGEHYALEVKGDSMIEAGINDGDVVVIRETSTADNGDIVVALVDDSEATLKRFFRRGASIALEAANPAYETRVLPSDRVRVQGRLVGLIRTY

Gene
lexA
Protein
LexA repressor
Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.438 kDa
Sequence
MLTRKQYELLRFISERLKESGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELQAAAGNRRGFTPSVIEGNLGKVRASSSADEGERPVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGSGEHYALEVRGDSMVEAGILDGDMALIQRNESADTGDIVVALIDDEEATLKRFRRRGASIALEPANAAYEVRILPPNRVKIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.438 kDa
Sequence
MLTRKQYELLRFISERLKESGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLPNRARAIEVIKLPELQAAAGNRRGFTPSVIEGNLGKVRASSSADEGERPVAVPVMGRIAAGTPIEALQTRSHTISVPPDMLGSGEHYALEVRGDSMVEAGILDGDMALIQRNESADTGDIVVALIDDEEATLKRFRRRGASIALEPANAAYEVRILPPNRVKIQGKLIGLYRKY

Gene
lexA
Protein
LexA repressor
Organism
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.114 kDa
Sequence
MLTRKQIELLEFIHKRLQRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHKARAIEIVKLPEALMGSMQGGFAPQVIDGDRLDPPVGAMPVSGIHAVELPVMGKIAAGTPIEAISEVSHTVAVPGQMMRQDAEHYALEVKGDSMINAGINNGDIVVIRETSVAESGDIVVALVDGHEATLKTLRKRGNAIALEAANPAYETRVYPAEMVRVQGKLVGLIRSY

Gene
lexA
Protein
LexA repressor
Organism
Acidiphilium cryptum (strain JF-5)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.593 kDa
Sequence
MLTRKQHELLVYIDQHLRRTGCSPSFEEMKEALDLKSKSGIHRLIGALEERGFLRRHKHRARALEVLRLPSDAAADRPDTGFAPNVIRGDFTARLQGARAADPAAAITLPLYGRIAAGQPIEALREHQAEIEIPASLVGPGEHYALEVAGDSMVDAGILDGDTAIIRRGETAETGQIVVALIDDVEVTLKRLRRRGNSTALEPANPRYEIRIFPAERVKVQGRLVALFRRY

Gene
lexA
Protein
LexA repressor
Organism
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.48 kDa
Sequence
MTDRKEHKMKPGRRPTEGMTPSQERIMQVIRNAIDRDGLPPTVKEIAEALGMKTPSAHEQVQKLVKKGFIRRTPRKARSIEIVEQSPEEEPVEKKPDVARLVPVPIIGEVAAGIPILAVENHIGELLMDSRTARGPCFALKVKGDSMIDAEIFEGDYVVVRHQALAENGDIVVAILDGEATVKRLYISEETIELRPENRSYQPIVVPPGGDIRILGKVLAVRGHGAANNNE

Gene
lexA
Protein
LexA repressor
Organism
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6)
Length
231 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.315 kDa
Sequence
MQDSPKLTARQQQILDLIQSTIERTGAPPTRAEIATEFGFRSANAAEEHLQALARKGVIELLGGTSRGIRLKSDTLRSINESRLRGIGQQFSLPLSNMPPAQLTLPLVGRVAAGSPILAQQHIDQSYTFEAHMFSRKPDFLLKVRGMSMRDAGILDGDLIAVQRASEAKNGQIVVARLGDEVTVKRWRRSKSGIDLIPENPDFDIIHVPADSPDFALEGLAVGLIRNTMLM

Gene
lexA
Protein
LexA repressor
Organism
Anaeromyxobacter sp. (strain K)
Length
230 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.114 kDa
Sequence
MEGLTDRQLEVLRFIASQIEDHGYPPTIREIGEALDIRSTNGVNDHLKALERKGYLSRDPVKSRALIPTSAAREALGGGGGDAGSNVVPLVRGPARPGSRMIEIPIVGRVAAGMPILAQERVEDTVQVDAFLLGTNKKVYGLRVQGDSMIGDGILPGDYVFVKKQLNADDGEIVVAMIDDEATVKRVYFEGDRVRFQPSNPRMAPIYVRHSDFRSTMILGVVVGVYRKLT

Gene
lexA
Protein
LexA repressor
Organism
Sorangium cellulosum (strain So ce56)
Length
230 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.198 kDa
Sequence
MQGLTERQQQVLHYIRQSISERGYPPTLREIGAHMGIRSTNGVNDHLRALERKGYLTREDMKSRALRPRDLDGAGAGGGADLRGALVNGGNDAPANDQEDDLVEIAVVGRIAAGLPILAEEHVLDTVRIERTLVRGGREVFGLRVTGDSMIEAGIFSGDYIFVRRQLTAQRGDIVVALIGDEATVKYFFPEKDYVRFQPANAAMAPILVRASDFKPAMLLGVVVGVYRKL

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium sp. (strain JLS)
Length
230 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.56 kDa
Sequence
MSDDSSETRTGGRRGADAGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRLSDEPATPVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQAVADNGDIVAAMIDGEATVKTFKRSRGQVWLMPHNPAFEPIPGNDAAVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium sp. (strain KMS)
Length
230 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.56 kDa
Sequence
MSDDSSETRTGGRRGADAGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRLSDEPATPVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQAVADNGDIVAAMIDGEATVKTFKRSRGQVWLMPHNPAFEPIPGNDAAVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium sp. (strain MCS)
Length
230 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.56 kDa
Sequence
MSDDSSETRTGGRRGADAGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRLSDEPATPVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQAVADNGDIVAAMIDGEATVKTFKRSRGQVWLMPHNPAFEPIPGNDAAVLGKVVTVIRKI

Gene
lexA
Protein
LexA repressor
Organism
Phenylobacterium zucineum (strain HLK1)
Length
229 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.099 kDa
Sequence
MLTRKQHELLMFIHERIKETGVSPSFDEMKEALDLASKSGIHRLITALEERGFLRRLPHRARALEVVRLPQQATAAAPPKGRAPFKPQLVEAGQAMPVAANDTRELPILGKIAAGTPIEAIQQERDRLPVPEAMLGAGEHFVLEIQGDSMINAGILDGDFVVIRRTDSANSGDIVVALVDGEEATLKRLRKKGASIALEAANPAYETRIFGPDRVAVQGRLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Phenylobacterium zucineum (strain HLK1)
Length
229 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.099 kDa
Sequence
MLTRKQHELLMFIHERIKETGVSPSFDEMKEALDLASKSGIHRLITALEERGFLRRLPHRARALEVVRLPQQATAAAPPKGRAPFKPQLVEAGQAMPVAANDTRELPILGKIAAGTPIEAIQQERDRLPVPEAMLGAGEHFVLEIQGDSMINAGILDGDFVVIRRTDSANSGDIVVALVDGEEATLKRLRKKGASIALEAANPAYETRIFGPDRVAVQGRLVGLIRRYH

Gene
lexA
Protein
LexA repressor
Organism
Anaeromyxobacter dehalogenans (strain 2CP-C)
Length
229 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.071 kDa
Sequence
MEGLTDRQLEVLRFIASQIEDHGYPPTIREIGEALDIRSTNGVNDHLKALERKGYLSRDPVKSRALIPTSAAREALGGGGEAGSNVVPLVRGPARPGSRMIEIPIVGRVAAGMPILAQERVEDTVQVDAFLLGTNKKVYGLRVQGDSMIGDGILPGDYVFVKKQLNADDGEIVVAMIDDEATVKRVYFEGDRVRFQPSNPRMAPIYVRHSDFRSTMILGVVVGVYRKLT

Gene
lexA
Protein
LexA repressor
Organism
Jannaschia sp. (strain CCS1)
Length
228 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.819 kDa
Sequence
MLTRKQRDLLEFIHKRMQRDGVPPSFDEMKEALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKMPDAMTGGGFEPRVIDGDRGPAPANAMAVRAAPAREVPVMGQIAAGVPIEAISQVASHVAVPEQMLGAGGNHYALEVKGDSMIDAGINDGDIVVIEEGNTADNGDIVVALVEDHEATLKRLRRKGGMIALEAANPAYETRVFRDDQVKVQGKLVGLIRTY

Gene
lexA
Protein
LexA repressor
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
228 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Has been shown to bind to the direct repeat sequence 5'-GTT-N(7)-GTTC-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.8 kDa
Sequence
MLTRKQMELLDFIKTRMDRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPEAMERAGFSARAAKAAAAPLPKGAVTVETAGALDLPLMGRIAAGLPIEAINGGPQSVTVPGMMLSGRGQHYALEVKGDSMIAAGINDGDIVVIREQQTADNGDIVVALVADHEATLKRYRRRGGMIALEPANDSYETQVYPEQMVKVQGRLVGLIRSY

Gene
lexA
Protein
LexA repressor
Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Length
228 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.25 kDa
Sequence
MLTRKQMELLDFIKTRMDRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPEAMERAGFAPRVIEGDRTEPPRGARPVETANALDLPLMGRIAAGLPIEAITDGAQSVTVPSMMLSGRGQHYALEVRGDSMIEAGINDGDIVVIREQQTADNGDIVVALVADHEATLKRFRRRGGMIALEPANASYETQVYPDHMVKVQGRLVGLIRSY

Gene
lexA
Protein
LexA repressor
Organism
Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258)
Length
228 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.044 kDa
Sequence
MEGLTDRQLEVLRFIASQIEDHGYPPTIREIGEALDIRSTNGVNDHLKALERKGYLSRDPVKSRALIPTSAAREALGGGETGSNVVPLVRGPARPGSRMIEIPIVGRVAAGMPILAQERVEDTVQVDAFLLGTNKKVYGLRVQGDSMIGDGILPGDYVFVKKQLNADDGEIVVAMIDDEATVKRVYFEGDRVRFQPSNPRMAPIYVRHSDFRSTMILGVVVGVYRKLT

Gene
lexA
Protein
LexA repressor
Organism
Hyphomonas neptunium (strain ATCC 15444)
Length
227 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.672 kDa
Sequence
MLTTKQKELLLFINDRIKDTGVSPSFDEMKEALDLASKSGIHRLITALEERGFIRRLANRARALEVLKLPDSAIPPPNARQRRDFRPALVTNQGAEAPRIAGMIPLVGRIAAGSPISAIQQENGQVASPGGLPEGDDYFALEVQGDSMIQAGILNGDTVILKRTNTAQTGDIVVALIDGEEATLKRLRRKGASVALEAANPAFETRIFGPDRVEVQGRLVALIRRYE

Gene
lexA
Protein
LexA repressor
Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Length
227 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.687 kDa
Sequence
MTRKQMELLDFIKTRMDRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPEAMERAGFSARAAKAAAAPLPKGAVTVETAGALDLPLMGRIAAGLPIEAINGGPQSVTVPGMMLSGRGQHYALEVKGDSMIAAGINDGDIVVIREQQTADNGDIVVALVADHEATLKRYRRRGGMIALEPANDSYETQVYPEQMVKVQGRLVGLIRSY

Gene
lexA
Protein
LexA repressor
Organism
Variovorax paradoxus (strain S110)
Length
227 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.859 kDa
Sequence
MQFAVKLTARQQQILDLIQSAIARTGAPPTRAEIANELGFKSANAAEEHLQALARKGVIELVSGTSRGIRLKGDALRSLNESRHREGGQFSLSLPGMSQLALPLIGRVAAGSPILAQEHVDQTYYVENTLFQRQPDYLLKVRGMSMRDAGIMDGDLLAVQATKEARNGQIVVARLGDEVTVKRLKRNKQVIELHAENPDYPTIVVQPGEPFEIEGLAVGLIRNTMLM

Gene
lexA
Protein
LexA repressor
Organism
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
Length
227 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
25.049 kDa
Sequence
MLTAKQHELLHFIQQRLDASGISPSFEEMKEALGLKSKSGIHRLISALEERGFLRRLPNRARALEVLKLPDTAKSVVTNNRDNVVQLRKAPSALKPIAANDIIEVPLHGRIAAGVPIEAFEDHEQLAVPAALLGSGEHYALEVSGDSMVEAGIFDGDYALIQKADTAREGDIVVALVDGQDATLKFFRREGKMIRLDPANSAYEPQRYPAERVIVQGRLSGLLRRYH

Gene
lexA
Protein
LexA repressor
Organism
Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382)
Length
226 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.308 kDa
Sequence
MTDERAAGGGATRRRKSLSDKQISILEFIQRTIAGQGYPPSMREIGDAVGLASLSSVTHQLNQLELSGYLRRDPNRPRALEVLIDLPGSGAAESGEPSTPVGDAAMVPMVGRIAAGIPITAEQMVEEVFPLPRQLVGKGDLFMLRVVGDSMIDAAICDGDWVVVRQQKTAENGDIVAAMLDDEATVKVFRQRDGHTWLLPRNSAFEPILGDFAEVVGKVVAVMRSV

Gene
lexA
Protein
LexA repressor
Organism
Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1)
Length
226 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.34 kDa
Sequence
MTDERAAGGGATRRRKSLSEKQISILEFIQRTIAGQGYPPSMREIGDAVGLASLSSVTHQLNQLELSGYLRRDPNRPRALEVLIDLPGTGTAESGEPSTPVGDAAMVPMVGRIAAGIPITAEQMVEEVFPLPRQLVGKGDLFMLRVVGDSMIDAAICDGDWVVVRQQKTAENGDIVAAMLDDEATVKVFRQRDGHTWLLARNSAFEPILGDFAEVVGKVVAVMRSV

Gene
lexA
Protein
LexA repressor
Organism
Halorhodospira halophila (strain DSM 244 / SL1)
Length
226 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.308 kDa
Sequence
MDTLTDRQREILELIRRSVAERGYPPTRAEICQSLGFRSPNAAESHLRALARKGAIEMRRGASRGIRLTDAFAGAAPEPSPATDDPNAGLPVVGRVAAGSPLLAEESIERYCQVDASLFSPPADYLLRVRGESMRDAGILDGDLLAVRRDTEARDGQIVVVRLHDEVTVKFLERCNGVLRLIPAHPDYPVIEVAADGQDAVLEGIGVGVLRSPLDPRGPEGNAASD

Gene
lexA
Protein
LexA repressor
Organism
Pelagibacter ubique (strain HTCC1062)
Length
225 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.905 kDa
Sequence
MLTKKQKNLLLFINKKLRASGVSPSYEEMKDSLNLKSKSGIHRLISALEERGFIRRLAHKARALEVIKLPETASANDIYNSFSPSVIKGGLDTENTNLNEMEIPVLGSIAAGTPVEAIQNEVSRIPLPSNLEKNGQYFGLKVQGDSMIEAGINEGDTVIIKRSDTADNGKIVVALIDEHEAMLKRIRRKGKTVALESANRNYETKIFGPDRVKVQGVLVSLYRNF

Gene
lexA
Protein
LexA repressor
Organism
Pelagibacter ubique (strain HTCC1062)
Length
225 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.905 kDa
Sequence
MLTKKQKNLLLFINKKLRASGVSPSYEEMKDSLNLKSKSGIHRLISALEERGFIRRLAHKARALEVIKLPETASANDIYNSFSPSVIKGGLDTENTNLNEMEIPVLGSIAAGTPVEAIQNEVSRIPLPSNLEKNGQYFGLKVQGDSMIEAGINEGDTVIIKRSDTADNGKIVVALIDEHEAMLKRIRRKGKTVALESANRNYETKIFGPDRVKVQGVLVSLYRNF

Gene
lexA
Protein
LexA repressor
Organism
Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
Length
225 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.699 kDa
Sequence
MDDAPKLTARQQQILDLVQTSIERTGSPPTRAEIAAELGFRSANAAEEHLQALARKGVIELVGGTSRGIRLKSDTLRSLNQLRNKQFSLPLPSLSQLMLPLVGRVAAGSPILAQEHIDQSYAIEASMFPRRPDYLLKVRGMSMRDAGILDGDLLAVQKAREAKNGQIVVARLGDEVTVKRFRRVRGTIELLPENPDFEPIVVTPESGEFEIEGLAVGLIRNTLLM

Gene
lexA
Protein
LexA repressor
Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.869 kDa
Sequence
MASKLTDRQQEILDLIRLTVSRTGFPPTRAEIARALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKDAGETIPPGPETAASALAGMADAVGRLLLPLVGRVAAGSPILAAEHVEREVGVDVDLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRHQGRIELLPENPDFSPIVVDGTQEFALEGIAVGLIRTQALH

Gene
lexA
Protein
LexA repressor
Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.869 kDa
Sequence
MASKLTDRQQEILDLIRLTVSRTGFPPTRAEIARALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKDAGETIPPGPETAASALAGMADAVGRLLLPLVGRVAAGSPILAAEHVEREVGVDVDLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRHQGRIELLPENPDFSPIVVDGTQEFALEGIAVGLIRTQALH

Gene
lexA
Protein
LexA repressor
Organism
Delftia acidovorans (strain DSM 14801 / SPH-1)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.217 kDa
Sequence
MLDHPKLTARQQQILDLIQAAISRTGAPPTRAEIANTLGFKSANAAEEHLQALARKGVIELVSGTSRGIRLRTDTVRNINAARGTSFGLPLSALAPLMLPLVGRVAAGSPILAQEHIDQTYSVEPSLFQTRPDYLLRVRGMSMRDAGIMDGDLLAVQSAHEARNGQIVVARLGDEVTVKRLRRTTQGVELLPENPDYPVIRVAPEEAFAIEGLAVGLIRNSMSM

Gene
lexA
Protein
LexA repressor
Organism
Acidovorax citrulli (strain AAC00-1)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.266 kDa
Sequence
MLDSPKLTARQQQILDLIQTAIARTGAPPTRAEIAAEFGFKSANAAEEHLQALARKGVIELVSGTSRGIRLRGEAVRSINAARGTQFHLPIPGISQLMLPLIGRVAAGSPILAEEHVDQTYSVEGSLFQHKPDYLLKVRGMSMRDAGIMDGDLLAVQSTREARNGQIIVARLGDEVTVKRLRRTAGAIELLPENPDYPIITVQPGESFEIEGLAVGLIRNTMLM

Gene
lexA
Protein
LexA repressor
Organism
Acidovorax ebreus (strain TPSY)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.186 kDa
Sequence
MLDSPKLTARQQQILDLIQTAIARTGAPPTRAEIAAELGFKSANAAEEHLQALARKGVIELVSGTSRGIRLRGETVRNINAARGAQFNLPIPGLSQLTLPLVGRVAAGSPILAQEHVDQTYTVEGSLFAHKPDYLLKVRGMSMRDAGIMDGDLLAVQATREARNGQIIVARLGDDVTVKRLRRTGSAIELLPENPDYPVIRVEPGEPFEIEGLAVGLIRNTMLM

Gene
lexA
Protein
LexA repressor
Organism
Verminephrobacter eiseniae (strain EF01-2)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.12 kDa
Sequence
MLDNPKLTARQQQVLDLIQNTMARTGAPPTRAEIAAELGFKSANAAEEHLQALARKGAIELVSGTSRGIRLHSETLRSIHAARSGPSGAGNPGSSPWVLPLIGRVAAGSPILAQEHVEQTYSVENGLFQHKPDYLLKVRGMSMRDAGIIDGDLLAVQATREARNGQIIVARLGDDVTVKRLRRTASTIELLPENPDYPVIVVQPGEPFEIEGLAVGLIRNTMLM

Gene
lexA
Protein
LexA repressor
Organism
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.442 kDa
Sequence
MLTRKQHELLCFINDRLLQTGVSPSFEEMKEALDLKSKSGVHRLISALEERNFIRRLPNRARALEVLRMPETATAKPTAAASGKAKAAAPAVPQAANENVLEIPLHGRIAAGLPIEALEGQSSLSVPAALLGPGEHYALEVAGDSMVEAGILDGDYALIRRAETARDGEIVVALIADAEATLKYFRREGAMIRLDPANRAYDPQRYKPDQVRIQGKLAGLLRRY

Gene
lexA
Protein
LexA repressor
Organism
Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.62 kDa
Sequence
MLGSPKLTARQQQILDLIQNAITLTGSPPTRAEIATELGFRSANAAEEHLQALARKGAIELVSGTSRGIRLKSEALRSINESRSKQFPLSLPGLSQLMLPLIGRVAAGSPILAQEHIDQTYYVESSLFQRKPDYLLKVRGMSMRDAGIMDGDLLAVQSTRDAKNGQIVVARLGDEVTVKRFRRTKDLIELCPENPDYQIIVVEPGEPFEIEGLAVGLIRNTMLM

Gene
lexA
Protein
LexA repressor
Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.506 kDa
Sequence
MSNENQTPRGTRRRKNLSEKQLAILDVIQRSVSQRGYPPSMREIGDAVGLSSLSSVTHQLNQLELSGYLRRDPNRPRALEILIDLPSAAAPDFESQTPVGDAAMVPLVGRIAAGVPITAEQQVEEVFPLPRQLVGNGELFMLKVVGESMIDAAICDGDWVVVRAQNTAENGDIVAAMLDEEATVKVFRQRDGHTWLLPRNSNFEPILGDFSQILGKVVAVLRAV

Gene
lexA
Protein
LexA repressor
Organism
Acidovorax sp. (strain JS42)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.186 kDa
Sequence
MLDSPKLTARQQQILDLIQTAIARTGAPPTRAEIAAELGFKSANAAEEHLQALARKGVIELVSGTSRGIRLRGETVRNINAARGAQFNLPIPGLSQLTLPLVGRVAAGSPILAQEHVDQTYTVEGSLFAHKPDYLLKVRGMSMRDAGIMDGDLLAVQATREARNGQIIVARLGDDVTVKRLRRTGSAIELLPENPDYPVIRVEPGEPFEIEGLAVGLIRNTMLM

Gene
lexA
Protein
LexA repressor
Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
Length
224 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.828 kDa
Sequence
MSDTPSKGPATGSLTERQRTILEVIRASVNERGYPPSIREIGDAVGLTSTSSVAHQLRTLEQKGFLRRDPNRPRAVDVRGIDDAGTPSATTDVIGSGDLPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGESMVDAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRTSGQVWLMPHNPLFEPIPGNDAAILGKVVTVIRKV

Gene
lexA
Protein
LexA repressor
Organism
Myxococcus xanthus (strain DK 1622)
Length
222 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.712 kDa
Sequence
MEELTERQREILSFIVKETETRGFPPTIREIGEHMDIRSTNGVNDHLKALERKGYLNRGEQQSRSLVATKRARLLLGLGARKDSGMVEIPLLGKVAAGAPLLAQENMEDSVKIDSFLLGGVNGREVFALRVKGQSMIDDGIHDGDYLFVKKTPSAQPGEIVVALIEDEATVKRYYPEGDRIRFQPANATMQPIYVSRAEFRSTMILGQVVGVYRKLQGGRTP

Gene
lexA
Protein
LexA repressor
Organism
Herminiimonas arsenicoxydans
Length
219 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.869 kDa
Sequence
MIKLTARQEQILNLIRDAIENTGFPPTRAEIAAELGFRSANAAEEHLQALARKGAIEISPGTSRGIRLRDMGGTRSDRSGAQLSLPHPALMQLNLPLVGRVAAGSPILAQEHIEATYNVDKSLFSAKPDFLLKVRGMSMRDAGILDGDLLAVKKIDSAKNGQIVVARLGDDVTVKRYKKTGSLIELLPENPDFQPIRVDLEHDDFALEGLAVGLMRTWN

Gene
lexA
Protein
LexA repressor
Organism
Janthinobacterium sp. (strain Marseille)
Length
219 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.03 kDa
Sequence
MIKLTARQEQILNLIRDAIENTGFPPTRAEIATELGFRSANAAEEHLQALARKGAIEISPGTSRGIRLRDMGNGDERFPGRQMALPHPALMQLSLPLVGRVAAGSPILAQEHIEATYDVDRSLFSAKPDFLLKVRGMSMRDAGILDGDLLAVKKIDTAKNGQIVVARLGEEVTVKRYKKSGSLIELLPENPDFEPIRVDLAHDEFALEGLAVGLMRTWN

Gene
lexA
Protein
LexA repressor
Organism
Roseiflexus sp. (strain RS-1)
Length
218 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.28 kDa
Sequence
MRSSDQLSARQRDILGFIEEFTQEHGYPPSIREIQDGLRISSTSVVAYNLRALESKGLIDRDGRVSRGIKIKNMTPMPLSRAQGGRVPLLGVITAGQPLPNPEDTSTTAVEMIEVPVDLAPPEKLQNVYALKVRGHSMIDALIDDGDIVLMRYQETADNGQMVAVRIEDDNAVTLKRFYREGDKVRLQPANVTMEPIYVDAARVHIQGRVVGVLRSMW

Gene
lexA
Protein
LexA repressor
Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Length
218 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.767 kDa
Sequence
MATLTPRQQQIFDLIRDTIRNTGFPPTRAEIAAEFGFSSPNSAEEHLRALARKGVIELTPGASRGIRLKVTRSDSERPDQFSLPMPGVLQLTLPLVGRVAAGSPILAAEHIDRQYQVDASVFDERPDYLLRVRGLSMRDAGILDGDLLAVKKASEAANGKVVVARLGDDVTVKRLKKRGDTIELIAENPDFQNIVLHAGRDEFSLEGIAVGLIRSSGF

Gene
lexA
Protein
LexA repressor
Organism
Cupriavidus necator
Length
218 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.767 kDa
Sequence
MATLTPRQQQIFDLIRDTIRNTGFPPTRAEIAAEFGFSSPNSAEEHLRALARKGVIELTPGASRGIRLKVTRSDSERPDQFSLPMPGVLQLTLPLVGRVAAGSPILAAEHIDRQYQVDASVFDERPDYLLRVRGLSMRDAGILDGDLLAVKKASEAANGKVVVARLGDDVTVKRLKKRGDTIELIAENPDFQNIVLHAGRDEFSLEGIAVGLIRSSGF

Gene
lexA
Protein
LexA repressor
Organism
Cupriavidus necator (strain JMP 134 / LMG 1197)
Length
218 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.742 kDa
Sequence
MATLTPRQQQIFDLIRNTIRNTGFPPTRAEIAAEFGFSSPNAAEEHLRALARKGVIELTPGASRGIRLKVARSDSEMPDQFSLPVSGIMQLTLPLVGRVAAGSPILAAEHIDRQYQVDASVFDERPDYLLRVRGLSMRDAGILDGDLLAVRKASEAPNGKIVVARLGDDVTVKRLQRRDGAIELIAENPDFPNIMVTPGREEFSLEGIAVGLIRSSGF

Gene
lexA
Protein
LexA repressor
Organism
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Length
217 amino acids
Function
Probably represses a number of genes involved in the response to DNA damage (SOS response), including itself, recA, uvrA, ruvAB and ssb (PubMed:15528664). The probable consensus LexA box is 5'-TGCAC-N4-GTGCA-3' (PubMed:15528664). In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair (Probable).
Similarity
Belongs to the peptidase S24 family.
Mass
24.288 kDa
Sequence
MENTNEKRKEMTARQEEIYEYIKKYSKENHMPPTVREIGNHFDISSTNGVRSILAALIKKGYINRSPRLSRGIEILSDDKESSKEVASNTIEIPIVGRVAAGTPILAVQNLEGTVTIDRDFLACRSDVFALRVKGDSMINAGIFDGDLIFARQQKTADLGEIVVAQIDNEATVKYYHPSADHVELRPANPKYKPIIVNNRKDFSIAGRVIGVMRKVN

Gene
lexA
Protein
LexA repressor
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Length
217 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.635 kDa
Sequence
MATLTPRQQQIFDLIRNTIRRTGFPPTRAEIAAEFGFSSPNAAEEHLRALARKGVIELTPGASRGIRLKVAHSDSEMPDQFSLPMAGVMQLTLPLVGRVAAGSPILAAEHIDRQYQVDASVFDERPDYLLRVRGLSMRDAGILDGDLLAVRRASEAANGKIVVARLGDDVTVKRLQRRGGHIELIAENPDFTNIIVEPGEEFSLEGIAVGLIRSSGF

Gene
lexA
Protein
LexA repressor
Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1)
Length
217 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.634 kDa
Sequence
MATLTPRQQQIFDLIRNTIRRTGFPPTRAEIAAEFGFSSPNAAEEHLRALARKGVIELTPGASRGIRLKVSRSDSELPDQFSLPMAGVLQLTLPLVGRVAAGSPILAAEHIDRQYQVDASVFDERPDYLLRVRGLSMRDAGILDGDLLAVRRASEAANGKIVVARLGDDVTVKRLQRRGGHIELIAENPDFTNIIVEPGEEFSLEGIAVGLIRSSGF

Gene
lexA
Protein
LexA repressor
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Length
217 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.358 kDa
Sequence
MLTRKQHDLLLFIHNRLSVSGISPSFEEMKLALDLKSKSGIHRLIKALEERGFIRRLPNRARALEVIRLPEDKTEIQKKISRDYTPPKADNDVIEIPLHGRIAAGLPIEALEGQSHLAVPPSYLGSGAHYALEVAGDSMVDAGIFDGDYIIVRQTDEAHEGEIVVALIDNSDATLKYFHREGRMVRLDPANRAYAPMRYDASRIGIQGRLVGLLRRY

Gene
lexA
Protein
LexA repressor
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.217 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDSATPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFAPIVVANTDEFALEGIAVGLIRTQPLH

Gene
lexA
Protein
LexA repressor
Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.246 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDNAAPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFTQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFSPIVVANTDDFALEGIAVGLIRTQPLH

Gene
lexA
Protein
LexA repressor
Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.217 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDSATPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFAPIVVANTDEFALEGIAVGLIRTQPLH

Gene
lexA
Protein
LexA repressor
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.217 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDSATPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFAPIVVANTDEFALEGIAVGLIRTQPLH

Gene
lexA
Protein
LexA repressor
Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.246 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDNAAPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFTQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFSPIVVANTDDFALEGIAVGLIRTQPLH

Gene
lexA
Protein
LexA repressor
Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.217 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDSATPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFAPIVVANTDEFALEGIAVGLIRTQPLH

Gene
lexA
Protein
LexA repressor
Organism
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.503 kDa
Sequence
MTKLTARQQQVFDLIRRAIERTGFPPTRAEIAAELGFSSANSAEEHLRALARKGVIELAAGASRGIRLIAGQDDLPHQFTLPHASIMQLSLPLVGRVAAGSPILAQEHISQTYMCDPSLFSSKPDYLLKVRGLSMRDAGIFDGDLLAVQKKSEAKDGQIIVARLGDDVTVKRLKRRPDGLELIAENPDYENIFVQAGSAEFALEGIAVGLIRPSEF

Gene
lexA
Protein
LexA repressor
Organism
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.476 kDa
Sequence
MTKLTARQQQVFDLIRRAIERTGFPPTRAEIAAELGFSSANSAEEHLRALARKGVIELAAGASRGIRLLAGPEDSPHQFTLPHASIMQLSLPLIGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGIFDGDLLAVQKRSEAKDGQIIIARLGDDVTVKRLKRRPNGLELIAENPDYENIFVETGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Paraburkholderia xenovorans (strain LB400)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.434 kDa
Sequence
MTKLTARQQQVFDLIRRAIERTGFPPTRAEIAAELGFSSANSAEEHLRALARKGVIELAAGASRGIRLLAGPEDSPHQFTLPHASIMQLSLPLIGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGIFDGDLLAVQKKSEAKDGQIVIARLGDDVTVKRLKRRPNGLELIAENPDYENIFVETGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Ralstonia pickettii (strain 12J)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.616 kDa
Sequence
MATLTPRQQQIYDLIRQTIQRTGFPPTRAEIAAEFGFSSPNAAEEHLRALARKGVIELTPGASRGIRLRAAGDTAQHQFSLPSMGLMQLTLPLVGRVAAGSPILAAEHIDRQYQVDPSLFSAQPDFLLKVRGMSMRDAGILDGDLLAVQRASEATNGKIVVARLGDDVTVKRFQRKGRHVELIAENPDFEPIHVDLDRDEFHLEGLAVGLIRPAAP

Gene
lexA
Protein
LexA repressor
Organism
Ralstonia solanacearum (strain GMI1000)
Length
216 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.536 kDa
Sequence
MATLTTRQQQIYDLIHQTIQRTGFPPTRAEIAAEFGFSSPNAAEEHLRALARKGVIELTPGASRGIRLRAEGGASPHQFSLPSMGLMQLTLPLVGRVAAGSPILAAEHIDRQYQVDPSLFSSRPDFLLKVRGMSMRDAGILDGDLLAVQRAAEAANGKIVVARLGDDVTVKRFQRKGRQVELIAENPDFEPIHVDLDRDEFQLEGLAVGLIRPAAP

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia pseudomallei (strain 1106a)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia pseudomallei (strain 1710b)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia pseudomallei (strain 668)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia pseudomallei (strain K96243)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.169 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGLDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRAEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.254 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDMPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGIELIAENPDYENIFVKAGSAEFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.175 kDa
Sequence
MAKKNSNKQQEILDYVYKCVHENGYPPSVREICSAVGFKSTSTVHSYLQKLIDKGHLQKDPTKPRAIKILNKTSQVQENRTNKEGYYTSREMVDVPVVGRVTAGQPILAVENITDTFPLPVDFVQNSDAFMLRIQGESMIDAGILDKDFVLVRQQSSANNGDIVVALIGDEATCKTFYREKDHIRLQPQNSSMEPIVVKDELSILGKVIGVFRRM

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia ambifaria (strain MC40-6)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.194 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSAEFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia cenocepacia (strain AU 1054)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.18 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSADFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia cenocepacia (strain MC0-3)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.18 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSADFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia cenocepacia (strain HI2424)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.18 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSADFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.18 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGVDDAPHQFTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSADFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.208 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIEDAPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSAEFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.194 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFTSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGLELIAENPDYENIFVKAGSAEFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.094 kDa
Sequence
MTKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGGDDAPHQFTLPHAGLMQLSLPLVGRVAAGSPILAQEHISQHFACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLMRRPGGIELIAENPDYENIFVKAGSADFALEGIAVGLIRSGEL

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia mallei (strain NCTC 10247)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia mallei (strain NCTC 10229)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia mallei (strain ATCC 23344)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Burkholderia mallei (strain SAVP1)
Length
215 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.199 kDa
Sequence
MIKLTARQQQVFDLIRRAIERSGFPPTRAEIAAELGFSSPNAAEEHLRALARKGVIELAAGASRGIRLLGIDDAPHQLTLPHAALMQLSLPLVGRVAAGSPILAQEHISQHYACDPALFSSKPDYLLKVRGLSMRDAGILDGDLLAVQKRTEAKDGQIIVARLGDDVTVKRLKRRPGGVELIAENPDYENIFVKAGSAEFALEGIAVGLIRPGEF

Gene
lexA
Protein
LexA repressor
Organism
Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95)
Length
214 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.653 kDa
Sequence
MSGLSQRQQRIYDYIKQFIRTNGYAPAIRDIQRELSISSTSVVAYNLRALESKGHIRREGNISRAIELINAEQPLPTVLGGQRVPVLGVIAAGQPIPVPNDSANSDDSVLVPEEIVGNDKLGDVYALRVKGYSMVDALIADGDIVLLRYQATAENGEMVAARIRDENEVTLKRIYWEGDRVRLQPANVTMEAMYYPSTNVEVQGRVVGVIRNLG

Gene
lexA
Protein
LexA repressor
Organism
Desulfotomaculum reducens (strain MI-1)
Length
214 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.884 kDa
Sequence
MLNAREEEVLNVIIENVKLKGYPPSVREIGEAVGLSSSSTVHSYLKRLEQKGYLRRDPTKPRAIEVIMSELSKNPSSHPLTSELSRYSDEELISIPLLGEVAAGVPLLAVENYDEKVTLPRSFTGYGEFFMLSVRGDSMIEAGILPGDLVLVRRQESVSNGDIAVALLEDEATVKRFYKEKNRIRLQPENSLLSPIYVQEVKILGKVVGLMRKI

Gene
lexA
Protein
LexA repressor
Organism
Bordetella avium (strain 197N)
Length
213 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.906 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKDAEPTPSPILASLSQLLLPLVGRVAAGSPILAAEHVEREVGVDPSLFSQAPDYLLKVRGMSMRDAGILEGDLLAVKKSSEARNGQIIVARLGDDVTVKRLQRHGSRIELLPENPEFSPILVAPDDEFALEGVAVGLIRTHALH

Gene
lexA
Protein
LexA repressor
Organism
Bordetella avium (strain 197N)
Length
213 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.906 kDa
Sequence
MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKDAEPTPSPILASLSQLLLPLVGRVAAGSPILAAEHVEREVGVDPSLFSQAPDYLLKVRGMSMRDAGILEGDLLAVKKSSEARNGQIIVARLGDDVTVKRLQRHGSRIELLPENPEFSPILVAPDDEFALEGVAVGLIRTHALH

Gene
lexA
Protein
LexA repressor
Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Length
213 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
24.031 kDa
Sequence
MQNKINEKQQKILDFLNEQIEKNGYPPSVREICNAVGFKSTSTVHSYLEKLRKQGLIQKDPSKPRALKVINNKKNSKTDEPKNIYSGKELVEVPIIGKVTAGQPILAVENIEDTFPLPLDFVQNSTVFMLRVQGDSMIEAGIFDNDYIVVKQQSTANNGDIVVALIDDEATVKTFYKEKGFIRLQPANKFYDPIIVRDNLSILGKVIGVFRKM

Gene
lexA
Protein
LexA repressor
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Length
213 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.714 kDa
Sequence
MKPIKALTARQQEVFNFLKHHIETTGMPPTRAEISRELGFRSPNAAEEYLKALARKGVVEILSGTSRGIRLLVDTEESANDEDAGLPLIGRVAAGEPILAEQHIEGTYKVDADMFKPQADFLLKVYGQSMKDIGILDGDLLAVHSTKDVRNGQVIVARIEDEVTVKRLERKGDVVYLHAENEEFKPIVVNLKEQPNFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Xanthomonas campestris
Length
213 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.207 kDa
Sequence
MDLTDTQQAILALIAERIETDGVPPSQTEIARAFGFKGVRAAQYHLEALEQAGAIRRVPGQARGIRLAGAAAHARAAPAEEPVRDDVLRLPVLGRVAAGLPIGADIGSDDFVVLDRVFFSPSPDYLLKVQGDSMRDEGIFNGDLIGVHRTRDARSGQIVVARIDEEITVKLLKIGKDRIRLLPRNPDYAPIEVLPDQDFAIEGLYCGLLRPNR

Gene
lexA
Protein
LexA repressor
Organism
Xanthomonas citri
Length
213 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Has been shown to bind to the palindromic sequence 5'-CTG-N(8-12)-C-[TC]-G. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair (By similarity).
Similarity
Belongs to the peptidase S24 family.
Mass
23.24 kDa
Sequence
MDLTDTQQAILALIAERIDADGVPPSQTEIARAFGFKGIRAAQYHLEALEHAGAIRRVPGQARGIRLAGQGAQTRTAPVSEVARDDVLRLPVLGRVAAGLPIGADIGSDDFVVLDRVFFSPSPDYLLKVQGDSMRDEGIFNGDLIGVHRTRDARSGQIVVARIDEEITVKLLKIGKDRIRLLPRNPDYAPIEVLPDQDFAIEGLYCGLLRPNR

Gene
lexA
Protein
LexA repressor
Organism
Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)
Length
212 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.134 kDa
Sequence
MSRSLTSRQQHVFDFIVKTMNELGYPPTRAEIARALGFRSPNAAEEHLRALDRKGVIRMIPGTSRGIRLTGEEDAAATSTDGLPVVGEVAAGSPILAAAHIDRHCPLAPDYFTPRADYLLRVRGLSMKDAGILDGDLLAVHRTQQIRDGQIVVARLDDEVTVKRFKRQGHHVWLVAENADFAPIEVDLRHQDLEIEGLGVGVIRGGGGNGLH

Gene
lexA
Protein
LexA repressor
Organism
Oenococcus oeni (strain ATCC BAA-331 / PSU-1)
Length
212 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.306 kDa
Sequence
MAETKQLGILRFIYEKQNEKGYPPTVREIGEAVGLSSTSTVHGHIDRLEKHGLLHKDPTKPRAIEITEKGLRALGVPETPGKVPIIGLVTAGMPILAVEQAATEFLPIPSDLERFDGDLFVLRVSGTSMINIGILDGDMVFVRKQDYADNGDIVVAMTTDFGNGEGEATVKRFFKESNHYRLQPENDTMAPIIVKNVSILGKVVGLYRNSIY

Gene
lexA
Protein
LexA repressor
Organism
Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / NCDO 523)
Length
212 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.361 kDa
Sequence
MAITQESKQIQVLRFIHEAQSENGYPPTVREIGEAVGLSSSSTIHGHIERLVKKGYLLKDASKPRARAIEVTDIGLEMLGISTTPGKIPVLGMVTAGTPILAVEEEATEFFPIPDNLMQFDGDLFMLNVHGDSMVNIGILDGDKVIVRKQENADNGDVVVAMNDNNEATVKRFFREADHYRLQPENNSMAPIILQKVSILGKVIGLYRDAIY

Gene
lexA
Protein
LexA repressor
Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.623 kDa
Sequence
MSRKHLTARQQEIFDFLKHHIDTTGMPPTRVEIAREIGFKSPNAAEEHLKALARKGYIEMLSGTSRGIRILINNDNEDVTQDLSLPLIGKVAAGTPIMAIEHVESHYPVNGAMFNPNADYLLKVNGNSMEKIGILDGDLLAVHKTNFARNGQVVVARVEDEVTVKRLEKKGELIYLHPENDELQPIIVDPRLKYIEIEGIAVGVIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Peptoclostridium difficile (strain 630)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.473 kDa
Sequence
MYLDLTEKQVLILEFIKSQIILKGYPPAVREICTAVGLRSTSTVHSHLNKLEKLGYIRKDPTKPRAIEVLERSKVNDVSGANQEIIELPLVGQITAGEPILAQQNIEEYIPFPASLVKGSNNFVLRVKGESMINAGILDEDYVVVDKKNTALNSQIVVALINGESATVKRFFKEGNLIRLQPENDFMEPIMLNDSEVEIVGIVTGVFRVIK

Gene
lexA
Protein
LexA repressor
Organism
Peptoclostridium difficile (strain 630)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.473 kDa
Sequence
MYLDLTEKQVLILEFIKSQIILKGYPPAVREICTAVGLRSTSTVHSHLNKLEKLGYIRKDPTKPRAIEVLERSKVNDVSGANQEIIELPLVGQITAGEPILAQQNIEEYIPFPASLVKGSNNFVLRVKGESMINAGILDEDYVVVDKKNTALNSQIVVALINGESATVKRFFKEGNLIRLQPENDFMEPIMLNDSEVEIVGIVTGVFRVIK

Gene
lexA
Protein
LexA repressor
Organism
Stenotrophomonas maltophilia (strain R551-3)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.159 kDa
Sequence
MDLTDTQQAILQLIAERIESEGAPPSQTEIARAFGFKGVRAAQYHLEALEQAGAIRRIPGQARGIRLVQAPPLEKLAEPGLPDNVLRLPVLGRVAAGLPIGADIGSDDFVVLDRVFFSPAPDYLLKVQGDSMIDEGIFDGDLIGVHRTRDAHSGQIVVARIDDEITVKLLKIAKDRIRLLPRNPDYKPIEVLPDQDFSIEGLYCGLLRPNR

Gene
lexA
Protein
LexA repressor
Organism
Pasteurella multocida (strain Pm70)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.506 kDa
Sequence
MKPFKALTARQQEVYDLLKRHLENTGMPPTRAEISKELGFRSPNAAEEHLKALARKGVIEIISGTSRGIRLLLEESESDENQGLPLVGRVAAGEPILAEQHIEGTYQVDANMFKPQANFLLKVYGQSMKNIGILDGDLLAVHSTKDVRNGQIVVARIEDEVTVKRLERKGSVIYLHAENEEFAPIVVDLNQQPNFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.54 kDa
Sequence
MIDSTTELRPLTKRQQQIYDLIKAKIQDTGMPPTRAEIANFFGFKSANAAEEHLKALAKKGYIEMLAGTSRGIRLVEEMLEAEGLPLIGRVAAGEPILAQEHIEEHYKMDGNLFHPAADYLLRVNGESMKDIGILDGDLLAVHQTTEVQNGQVVVARVENDVTVKRFKREGNVVYLHAENEDFSPIKVDLANQEFNIEGIAVGIIRSGRWM

Gene
lexA
Protein
LexA repressor
Organism
Leuconostoc citreum (strain KM20)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.142 kDa
Sequence
MAIQESKQIQVLRFIHEAQLNNGYPPTVREVGEAVGLSSSSTIHGHIERLVKKGYLLKDASKPRARAIEVTDSGLEALGVSTTPGRIPVLGQVTAGAPILAVEEEATEFFPIPDNLMQFDGDMFMLNVRGNSMINIGILDGDKVIVRKQDNADNGDVVVAMNDDDEATVKRFFREADHFRLQPENDAMAPIILKQVAILGKVIGLYRDAIY

Gene
lexA
Protein
LexA repressor
Organism
Xylella fastidiosa (strain M23)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.323 kDa
Sequence
MSLSDIQQAILSLITNNINADGVSPSQTEIARAFGFKGVRAVQHHLDVLEQQGMIRRIPGQARGIRLKHLTEVDEVALALQSKDVLRLPVLGRVAAGQPIGADIGEDHVVLLDRVFFSPAPDYLLRVQGDSMRDEGIFDGDLIGVHRTQDAHSGQIVVARIDDEITVKLLKISKDRIRLLPRNPDFAPIEVRSDQDFAIEGLYCGLLRPNR

Gene
lexA
Protein
LexA repressor
Organism
Xylella fastidiosa (strain 9a5c)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.395 kDa
Sequence
MSLSDIQQAILSLITNHINADGVSPSQTEIARAFGFKGVRAVQHHLDVLEQQGMIRRVPRQARGIRLKHLTEVDETALALQSEDVLRLPVLGRVAAGQPIGADIGEGRVVLLDRVFFSPAPDYLLRVQGDSMRDEGIFDGDLIGVHRTQDAHSGQIVVARIDDEITVKLLKISKDRIRLLPRNPDFAPIEVRSDQDFAIEGLYCGLLRPNR

Gene
lexA
Protein
LexA repressor
Organism
Xylella fastidiosa (strain M12)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.332 kDa
Sequence
MSLSDIQQAILSLITNHINADGVSPSQTEIARAFGFKGVRAVQHHLDVLEQQGMIRRVPGQARGIRLKHLTQVDEAALALQSEDVLRLPVLGRVAAGQPIGADIGEDRVVLLDRVFFSPAPDYLLRVQGDSMRDEGIFDGDLIGVHRTHDAHSGQIVVARIDDEITVKLLKISKDRIRLLPRNPDFAPIEVRSDQDFAIEGLYCGLLRPNR

Gene
lexA
Protein
LexA repressor
Organism
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Length
211 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.323 kDa
Sequence
MSLSDIQQAILSLITNNINADGVSPSQTEIARAFGFKGVRAVQHHLDVLEQQGMIRRIPGQARGIRLKHLTEVDEVALALQSKDVLRLPVLGRVAAGQPIGADIGEDHVVLLDRVFFSPAPDYLLRVQGDSMRDEGIFDGDLIGVHRTQDAHSGQIVVARIDDEITVKLLKISKDRIRLLPRNPDFAPIEVRSDQDFAIEGLYCGLLRPNR

Gene
lexA
Protein
LexA repressor
Organism
Haemophilus somnus (strain 129Pt)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.49 kDa
Sequence
MSSIKSLTTRQQEVFDLIKRHIESTGMPPTRVEISKELGFRSPNAAEEHLKALARKGVIEIVSGVSRGIRLLTDIEEPENEGLPLIGRVAAGEPILAEQHIEATYQVDANMFKPQADFLLKVYGQSMKDIGILDGDLLAVHSTKDIRNGQIVVARIEDEVTVKRFERKGSVVYLHAENEEFEPIVVDLTQQPYFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Histophilus somni (strain 2336)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.49 kDa
Sequence
MSSIKSLTTRQQEVFDLIKRHIESTGMPPTRVEISKELGFRSPNAAEEHLKALARKGVIEIVSGVSRGIRLLTDIEEPENEGLPLIGRVAAGEPILAEQHIEATYQVDANMFKPQADFLLKVYGQSMKDIGILDGDLLAVHSTKDIRNGQIVVARIEDEVTVKRFERKGSVVYLHAENEEFEPIVVDLTQQPYFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Koribacter versatilis (strain Ellin345)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.047 kDa
Sequence
MVALTRRQREMYDFLCSFTDSHGYSPSFEEIAEGMGLSSLATVHKHIGNLESKGLLKRDYNRARSIEVLRPKGQLKKSMAAAAAVATAGLPFLGRIAAGQPIEAIENPETISLGDFTGSKEVFVLQVSGESMQDEHIVDGDYVLVERINTARDGEIVVALVENSDTTLKRIYREGETVRLQPSNAKMQPIRVPAGSVQVQGRVIGVLRKY

Gene
lexA
Protein
LexA repressor
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.351 kDa
Sequence
MPPELTPTRRSILQATLRLGAGATAGQVAQEVGITKQAISQQVNILRKLGYLQPAETRYGPLQVTDRARAALGEGLPIYGQIAAGIPALAEQSPEDFTPSIEALLGLKAGDFLLRVRGESMTGIGVMDGDYVVVRPAPEVHDGEVAVVLVPGDNAATLKRLYHFGQDILLTSENPAMPRLSFPAEQVQVQGRMVGRVGVGAPRVSHRVTE

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.302 kDa
Sequence
MSKTSESKQMAVLRFIYERVNEKGYPPTVREIGEAVDLSSTSTVHGHISRLEKKGYIQKDPTKPRAIEVTPAGFEALGVETTPHQIPVLGTVTAGQPILAVQEATDYFPIPKELESFGGDLFMLTIRGESMINIGIMNGDQVIVRRQSSADNGDIIIAMTDENEATCKRFFKEADHYRLQPENDTMAPIILNNVSVLGKVVGLYRDMLFQ

Gene
lexA
Protein
LexA repressor
Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.369 kDa
Sequence
MSRKHLTARQQEIFDFVKHHIETTGMPPTRVEIAREIGFKSPNAAEEHLKALARKGYIEMLSGTSRGIRILVDNEETAANDDGLPLIGKVAAGTPIMAIEHVESHYPVNGAMFNPNADYLLKVNGNSMEKIGILDGDLLAVHKTNFARNGQVVVARVDDEVTVKRLEKKGDLIYLHPENDELQPIIVDPRIEYIEIEGIAVGVIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.355 kDa
Sequence
MSRKHLTARQQEIFDFVKHHIETTGMPPTRVEIAREIGFKSPNAAEEHLKALARKGYIEMLSGTSRGIRILVDNEETAANDDGLPLIGKVAAGTPIMAIEHVESHYPVNGAMFNPNADYLLKVNGNSMEKIGILDGDLLAVHKTNFARNGQVVVARVDDEVTVKRLEKKGDLIYLHPENDELQPIVVDPRIEYIEIEGIAVGVIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.369 kDa
Sequence
MSRKHLTARQQEIFDFVKHHIETTGMPPTRVEIAREIGFKSPNAAEEHLKALARKGYIEMLSGTSRGIRILVDNEETAANDDGLPLIGKVAAGTPIMAIEHVESHYPVNGAMFNPNADYLLKVNGNSMEKIGILDGDLLAVHKTNFARNGQVVVARVDDEVTVKRLEKKGDLIYLHPENDELQPIIVDPRIEYIEIEGIAVGVIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)
Length
210 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.387 kDa
Sequence
MSLVKPLTARQQEVYNFLKHYIETTGMPPTRAEISRELGFRSPNAAEEHLKALARKGAVEILAGTSRGIRLLLDAANDEPEGLPLIGQVAAGEPILAEQHIEGTYRVDPDMFKPQADFLLKVNGQSMKNIGILDGDLLAVHSTKDVRNGQVIVARIEDEVTVKRLERKGDVIYLHAENEEFAPIVVNLREQERFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.213 kDa
Sequence
MKRQHLTARQQEIFEFVKNHIESTGMPPTRVEIAREIGFKSPNAAEEHLKALARKGYIEMLSGTSRGIRILVEDEAANDEEGLPLIGKVAAGTPIEAIEHIEKHYPVNGAMFSPAADYLLKVNGNSMEKIGILDGDLLAVHKTKSVRNGQVVVARVDDEVTVKRLEKKGDLIYLHPENDELEPIVVDPRQSYIEIEGIAVGVIRSNAWM

Gene
lexA
Protein
LexA repressor
Organism
Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.918 kDa
Sequence
MAKNISTKQLSVLEYIYKTVNAQGYPPTVREIGSAIGLSSTSTVHGHIDRLQKNGFLEKDPTKPRALEVTKLGLDALGVQDKNPTIPLLGVVTAGEPILAVEEATDFFPVPPEYENDSSNLFMLTIRGESMINAGILSGDQVIVRKQSTADNGTIVIAMTDENEATCKRFYRESDHIRLQPENDTMAPIILDNVTILGKVVGLFRDNIY

Gene
lexA
Protein
LexA repressor
Organism
Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.918 kDa
Sequence
MAKNISTKQLSVLEYIYKTVNAQGYPPTVREIGSAIGLSSTSTVHGHIDRLQKNGFLEKDPTKPRALEVTKLGLDALGVQDKNPTIPLLGVVTAGEPILAVEEATDFFPVPPEYENDSSNLFMLTIRGESMINAGILSGDQVIVRKQSTADNGTIVIAMTDENEATCKRFYRESDHIRLQPENDTMAPIILDNVTILGKVVGLFRDNIY

Gene
lexA
Protein
LexA repressor
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.029 kDa
Sequence
MKPLTPRQQEVFDLIKSKIDETGMPPTRAEIAKELGFRSANAAEEHLKALARKQVIEMVPGASRGIRILVDNAANEEEAETGLPLIGRVAAGEPILAQEHVEAHYQVDPSMFRPQADFLLRVHGESMKNIGILDGDLLAVHKTQDVRNGQVVVARVEDDVTVKRLERKGSKVFLHAENEEFAPIEVDLAAQSLTIEGIAVGVIRNSTWM

Gene
lexA
Protein
LexA repressor
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.029 kDa
Sequence
MKPLTPRQQEVFDLIKSKIDETGMPPTRAEIAKELGFRSANAAEEHLKALARKQVIEMVPGASRGIRILVDNAANEEEAETGLPLIGRVAAGEPILAQEHVEAHYQVDPSMFRPQADFLLRVHGESMKNIGILDGDLLAVHKTQDVRNGQVVVARVEDDVTVKRLERKGSKVFLHAENEEFAPIEVDLAAQSLTIEGIAVGVIRNSTWM

Gene
lexA
Protein
LexA repressor
Organism
Vibrio cholerae serotype O1 (strain M66-2)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.029 kDa
Sequence
MKPLTPRQQEVFDLIKSKIDETGMPPTRAEIAKELGFRSANAAEEHLKALARKQVIEMVPGASRGIRILVDNAANEEEAETGLPLIGRVAAGEPILAQEHVEAHYQVDPSMFRPQADFLLRVHGESMKNIGILDGDLLAVHKTQDVRNGQVVVARVEDDVTVKRLERKGSKVFLHAENEEFAPIEVDLAAQSLTIEGIAVGVIRNSTWM

Gene
lexA
Protein
LexA repressor
Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.261 kDa
Sequence
MRVLAKRTETRQLEVLKYIYEQVELKGYPPTVREIGKAVDLSSTSTVHGHLARLEKKGLILRDPTKPRAIELTPEGLEKIGIQPTTIPMLGVVTAGEPILAVEEASDFFPLPPDLRTEENALFMLTIRGESMINAGILDGDQVIVRKQSNANNGDIVIAMTDEDEATCKRFFREVDHIRLQPENDALAPILLDNVTILGKVVGLYRNHI

Gene
lexA
Protein
LexA repressor
Organism
Psychromonas ingrahamii (strain 37)
Length
209 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.241 kDa
Sequence
MKELTKRQNEVLDVIKDQILKTGMPPTRVELAKILGFRSANAAEEHLKALARKGAIEILAGTSRGIRLLGEHQHNEKAHQDGLPLIGQVAAGEPILAQQHIETYYDVDPALFHPSADFLLRVQGESMKDIGIMDGDLLAVHKTQDIKNGQVVIARVEDDVTVKRFYREGRQVILKAENNDFGPIKIDLAYQSFDIEGIAVGVIRTADWM

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.015 kDa
Sequence
MSRKNSDTKQLEILRYIYDTVENRGFPPTVREICAAVGLSSTSTVHGHLSRLERKGFLIKDATKPRALEITAEGKTELGIKPKEIPVVGVVTAGQPILAVEDISEYFPLPPDLESDAGELFMLKVHGNSMIKAGILNGDNVIVRKQSTANNGEIVVAMTDENEATVKRFFKEDDHYRLQPENDTMAPIILQQVSILGKVVGLYRNNIQ

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus casei (strain BL23)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.786 kDa
Sequence
MPTQASQKRWKQILQSIYDAIEDHGYPPTVREIGKSVGLSSSSTVAAYLEKLLAAGLIAKDPAKPRTLEVTSAGRDFIGVQDHGIPIVGTVAAGVPITAIENIDDYFPVPDDLPYAADELFMLRVQGNSMIKIGILDGDQIIVKKQNDAENGQIVVAMTEEDEATVKRFYKEKNGIRLHPENDSMDDMFFPDVTILGIVVSLYRPALV

Gene
lexA
Protein
LexA repressor
Organism
Bacillus clausii (strain KSM-K16)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.179 kDa
Sequence
MSKLSKRQEEILAYIKDEVKKKGYPPSVREIGEAVGLASSSTVHGHLARLEKKGYIRRDPTKPRAIEVLSLGFDNDTFVKKETASFIPVIGKVTAGVPITAVENVEDYLPLPDHLAAYDNTYALVIQGESMIEAGIYDGDQVIVRQQQTADNGDIIVAMTEDNEATVKRFFREKDYIRLQPENSSMEPIILENCTILGKVIGVFRTIH

Gene
lexA
Protein
LexA repressor
Organism
Finegoldia magna (strain ATCC 29328)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.761 kDa
Sequence
MYDDLTSKQIEILKFIKRYIDYKGYPPAIREIGDSLNINSTSTVHNNILKLEMKGYLRRDPLKNRALEIIDSVYEEQENEIKKETIDVPIVGKVQAGMPILAIENVEDTFPLPIEYTSQGIVFILKVQGESMIEDGILNGDKIIVRKQNTANNGDIVVALMDESATVKRFYRHSDHIELRPSNSTMYPIIVKDVEILGKVIGLYRTIY

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus fermentum (strain NBRC 3956 / LMG 18251)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.697 kDa
Sequence
MPRNSTNKQMAVLSFIHKQVDAHGYPPTVREICGAVGLSSTSTVHGHINRLIKKGYLKKDPSKPRALEITPAGLEVLGITPKQTQIPLLGVVAAGEPILAVQDATDFFPIPPSIPDHDDLFMLTIQGTSMINIGILNGDKVIVRRQETANNGDIVIAMTSDNEATCKRFFKEQGHIRLQPENDTLAPIILDDVTILGKVVGLFRDDIF

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus helveticus (strain DPC 4571)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.177 kDa
Sequence
MSKKNSDTKQLEILRYIYDTVDHRGFPPTVREICAAVKLSSTSTVHGHLARLERKGLLIKDATKPRALEITDEGKKELGIKPKRIPVIGVVAAGHPILAVQDIDEYFPLPPDLENDAGELFMLKIHGESMINAGILNGDNVIVKKQNTANNGEIVVAMTDENEATVKRFYKEKDHYRLQPENDTMAPIILPEVTILGKVVGLYRNNID

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus paracasei (strain ATCC 334 / BCRC 17002 / CIP 107868 / KCTC 3260 / NRRL B-441)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.786 kDa
Sequence
MPTQASQKRWKQILQSIYDAIEDHGYPPTVREIGKSVGLSSSSTVAAYLEKLLAAGLIAKDPAKPRTLEVTSAGRDFIGVQDHGIPIVGTVAAGVPITAIENIDDYFPVPDDLPYAADELFMLRVQGNSMIKIGILDGDQIIVKKQNDAENGQIVVAMTEEDEATVKRFYKEKNGIRLHPENDSMDDMFFPDVTILGIVVSLYRPALV

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus reuteri (strain DSM 20016)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.184 kDa
Sequence
MAKLAKNKQMAVLNYIHKQVEDHGYPPTVREICSAVGLSSTSTVHGHISRLIEQGFLQKDPSKPRALEITPKGLDILGVKPIQKEIPMLGVVTAGQPILAVENATEFFPIPPSIQDNNDLFMLTIRGTSMIKAGIFNGDQVIVRKQSTAKNGDIVIAMNDDNEATCKRFYKEKTRFRLQPENDTMEPIFLDNVKILGKVVGLFRDHIF

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus reuteri (strain JCM 1112)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.184 kDa
Sequence
MAKLAKNKQMAVLNYIHKQVEDHGYPPTVREICSAVGLSSTSTVHGHISRLIEQGFLQKDPSKPRALEITPKGLDILGVKPIQKEIPMLGVVTAGQPILAVENATEFFPIPPSIQDNNDLFMLTIRGTSMIKAGIFNGDQVIVRKQSTAKNGDIVIAMNDDNEATCKRFYKEKTRFRLQPENDTMEPIFLDNVKILGKVVGLFRDHIF

Gene
lexA
Protein
LexA repressor
Organism
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.964 kDa
Sequence
MKPLTARQQEVFDLIKAKIDDTGMPPTRAEIARELGFRSANAAEEHLKALARKQVIEIIPGASRGIRILLQDADHHDEELGVPLIGQVAAGEPILAQEHVESHYKVDPGMFKPQADFLLRVNGESMKDIGIMDGDLLAVHKTQDVRDGQVVVARVDDDVTVKRLERKGSMVFLHAENEEFSPIEVDLTSQSLSIEGLAVGVIRSTTWM

Gene
lexA
Protein
LexA repressor
Organism
Aliivibrio fischeri (strain MJ11)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.942 kDa
Sequence
MKPLTARQQEVFDLIKAKIDDTGMPPTRAEIARELGFRSANAAEEHLKALARKQVIEIIPGASRGIRILLQDADDHDEELGVPLIGQVAAGEPILAQEHVESHYKVDPGMFKPQADFLLRVNGESMKDIGIMDGDLLAVHKTQDVRDGQVVVARVDDDVTVKRLERKGSMVFLHAENEEFSPIEVDLTSQSLSIEGLAVGVIRSTTWM

Gene
lexA
Protein
LexA repressor
Organism
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.068 kDa
Sequence
MTNDTLTPRQQQVLDQIRGHIRRTGYPPTRAEICRALGFRSPNAAEAHLRALARKGAIELRPGTSRGIHLPEEAAANDSDGLPVVGRVAAGSPILAEAHIDRHYRVDTHLFSPRPDYLLRVRGMSMRDAGILDGDLLVVHRTHEARNGQIVVMRLHDEVTVKRLEQHGSRLRLLAENPDYPTIEVDLTRDDASLEGIAVGVIRNEGLD

Gene
lexA
Protein
LexA repressor
Organism
Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype)
Length
208 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.976 kDa
Sequence
MRPLTARQTEVLELIKTTMQETGMPPTRAEIARQLGFRSANAAEEHLKALARKGVIEILPGTSRGIKLNIPLDNEAEEEEGLPLIGRVAAGEPILAQEHVESHYKVDPALFQPQADFLLRVNGMSMKDIGILDGDLLAVHRTTDVHNGQVVVARVDEDVTVKRLEKRGREVLLHAENEEFSPIKVDLANEPFAIEGIAVGVIRNADWM

Gene
lexA
Protein
LexA repressor
Organism
Haemophilus influenzae (strain PittEE)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.02 kDa
Sequence
MRPLTARQQEVLDLLKRHLETTGMPPTRAEISRELGFKSANAAEEHLKALSRKGAIEIIPGASRGIRILDNSSNDEFDGLPLVGRVAAGEPILAEQHIEATYRVDADMFKPQADFLLKVYGLSMKNVGILDGDLLAVHSTKDVRNGQIVVARIEDEVTVKRLEKKGSIIYLHAENEEFDPIVVNLEEQKNFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Haemophilus influenzae (strain PittGG)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.02 kDa
Sequence
MRPLTARQQEVLDLLKRHLETTGMPPTRAEISRELGFKSANAAEEHLKALSRKGAIEIIPGASRGIRILDNSSNDEFDGLPLVGRVAAGEPILAEQHIEATYRVDADMFKPQADFLLKVYGLSMKNVGILDGDLLAVHSTKDVRNGQIVVARIEDEVTVKRLEKKGSIIYLHAENEEFDPIVVNLEEQKNFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.105 kDa
Sequence
MRPLTARQQEVLDLLKRHLETTGMPPTRAEISRELGFKSANAAEEHLKALSRKGAIEIIPGASRGIRILDNSSNDEFDGLPLVGRVRAGEPILAEQHIEATYRVDADMFKPQADFLLKVYGLSMKNVGILDGDLLAVHSTKDVRNGQIVVARIEDEVTVKRLEKKGSIIYLHAENEEFDPIVVNLEEQKNFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.732 kDa
Sequence
MRPLTPRQAEILDLIKRNIAETGMPPTRAEIASRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLAGDELEDQPDPGLPLIGQVAAGEPILAQEHVEQYYQVDPAMFRPHADFLLRVRGDSMKDIGILDGDLLAVHKMNQARNGQVVVARVEDDVTVKRFEKQGNVVYLHAENEAFAPIRVDLANQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.134 kDa
Sequence
MSKLSRRQQEILDYIKEEVRAKGYPPSVREIGEAVGLASSSTVHGHLSRLEKKGYIRRDPTKPRAIEVLDLENLASETTEAKATYIPVVGKVTAGLPITAVENVEEYFPLPEQLTANDNTYALRIQGDSMIEAGIFDGDLVIVRQQQTADNGDIIVAMTEEDEATVKRFFREKDYIRLQPENSTMEPIILTTCTILGKVIGVFRTIH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.264 kDa
Sequence
MTKLSKRQLDILRFIKEEVKRKGYPPSVREIGEAVGLASSSTVHGHLARLETKGLIRRDPTKPRAIEILDTEEEIHIPKNQVVNVPVIGKVTAGTPITAVENIEEYFPLPERLAPPDEHVFMLEIMGESMIDAGILDQDYVIVKQQNTANNGDIVVAMTEDDEATVKRFFKEETHIRLQPENPTMEPIILQNVTILGKVIGVFRTVH

Gene
lexA
Protein
LexA repressor
Organism
Geobacillus kaustophilus (strain HTA426)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.187 kDa
Sequence
MTKLSKRQQQILEFIKQEVKTKGYPPSVREIGEAVGLASSSTVHGHLARLESKGYIRRDPTKPRAIEILDNDMAKEREKEEIISVPIIGKVTAGQPITAVENIEGYFPLPKRLAAGEEQLFMLEVMGDSMIEAGILDGDYVIVRQQSSANNGDIVVAMTEDNEATVKRFFKEKDHIRLQPENAHLEPIIVRDCTILGKVIGVYRLFD

Gene
lexA
Protein
LexA repressor
Organism
Geobacillus sp. (strain WCH70)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.086 kDa
Sequence
MTKLSKRQQQILDFIKKEVKTKGYPPSVREIGEAVGLASSSTVHGHLARLESKGYIRRDPTKPRAIEILDADFSASNQTDDVISVPIIGKVTAGQPITAIENIEDYFPLPKRLVSSEDHVFMLEVMGDSMIEAGILDGDYVIVRQQQSADNGDIVVAMTEDNEATVKRFFKEKDHIRLQPENSNLEPIIVRDCTILGKVIGVYRVIH

Gene
lexA
Protein
LexA repressor
Organism
Geobacillus thermodenitrificans (strain NG80-2)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.24 kDa
Sequence
MTKLSKRQQQILEFIKQEVKTKGYPPSVREIGEAVGLASSSTVHGHLARLESKGYIRRDPTKPRAIEILDSDLTKEREKEEVISVPMIGKVTAGQPITAVENIEDYFPLPKRLAAGEKQLFMLEVMGDSMIEAGILDGDYVIVRQQSSANNGDIVVAMTEENEATVKRFFKEKDHIRLQPENVHLEPIIVRDCTILGKVIGVYRLIN

Gene
lexA
Protein
LexA repressor
Organism
Haemophilus influenzae (strain 86-028NP)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.02 kDa
Sequence
MRPLTARQQEVLDLLKRHLETTGMPPTRAEISRELGFKSANAAEEHLKALSRKGAIEIIPGASRGIRILDNSSNDEFDGLPLVGRVAAGEPILAEQHIEATYRVDADMFKPQADFLLKVYGLSMKNVGILDGDLLAVHSTKDVRNGQIVVARIEDEVTVKRLEKKGSIIYLHAENEEFDPIVVNLEEQKNFEIEGIAVGIIRNNAWM

Gene
lexA
Protein
LexA repressor
Organism
Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.291 kDa
Sequence
MSKLSSRQQAIIEFIRKEVRDKGYPPSVREIGEAVGLASSSTVHGHLARLEKKGLIRRDPTKPRAIELLSDEDRFQDNFEDSVVRVPVIGKVTAGQPITAIEDVEEYFPLPDNIVTSDKVYMLRVSGNSMIDAGILDGDYVIVRQQHVANNGDIVVAMTEEDEATVKRFFKEKNHFRLQPENATMEPIILEHVTILGKVIGVYRLIH

Gene
lexA
Protein
LexA repressor
Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.915 kDa
Sequence
MRPLTPRQEEVLQLIKTTMLETGMPPTRAEIARHLGFKSANAAEEHLKALARKGAIEILPGTSRGIRLTEPLEDQLEDQGLPLIGRVAAGEPILAQEHVEMHYKVDPSLFKPSADFLLRVSGMSMKDIGILDGDLLAVHKTTDVHNGQVVVARVDEDVTVKRLERKGRQVVLHAENEDFQPIKVDLATQPFNIEGIAVGVIRNADWM

Gene
lexA
Protein
LexA repressor
Organism
Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.291 kDa
Sequence
MSKLSSRQQAIIEFIRKEVRDKGYPPSVREIGEAVGLASSSTVHGHLARLEKKGLIRRDPTKPRAIELLSDEDRFQDNFEDSVVRVPVIGKVTAGQPITAIEDVEEYFPLPDNIVTSDKVYMLRVSGNSMIDAGILDGDYVIVRQQHVANNGDIVVAMTEEDEATVKRFFKEKNHFRLQPENATMEPIILEHVTILGKVIGVYRLIH

Gene
lexA
Protein
LexA repressor
Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.915 kDa
Sequence
MRPLTPRQEEVLQLIKTTMLETGMPPTRAEIARHLGFKSANAAEEHLKALARKGAIEILPGTSRGIRLTEPLEDQLEDQGLPLIGRVAAGEPILAQEHVEMHYKVDPSLFKPSADFLLRVSGMSMKDIGILDGDLLAVHKTTDVHNGQVVVARVDEDVTVKRLERKGRQVVLHAENEDFQPIKVDLATQPFNIEGIAVGVIRNADWM

Gene
lexA
Protein
LexA repressor
Organism
Desulfovibrio alaskensis (strain G20)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.762 kDa
Sequence
MGRNREDDITPLQQETLDEICRYVSAKGYPPTVKEMSETFGISHASVHDRINQLVRKGYLKREEGKARGLTVTKHPQTNAVALVAVPIVGTVAAGHPIFAHENITGEVLVEASVVGSGKCFALYTQGDSMIDAGINDGDLIIVRRQPIAEDGDIVIALLDDEATVKRLKIDNELIELVPENPRLKPIRVKPEDELRILGKVVGRKRI

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.332 kDa
Sequence
MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain COL)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.301 kDa
Sequence
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain Newman)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.235 kDa
Sequence
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSFTVHGHLSRLEEKGYIEGDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.332 kDa
Sequence
MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain N315)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.332 kDa
Sequence
MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain MRSA252)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.301 kDa
Sequence
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain MSSA476)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.301 kDa
Sequence
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain MW2)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.301 kDa
Sequence
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus carnosus (strain TM300)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.148 kDa
Sequence
MTELTKRQSEIYEYIKTVVHTKGYPPSVREIGEAVGLASSSTVHGHLSRLESKGYIRRDPTKPRAIEIVSDQLEENAEMEGTIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEDDEATVKRFYKEKHRYRLQPENSTMDPIYLEQVTVLGKVVGLFREL

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.237 kDa
Sequence
MRELTKRQSEIYDYIKHVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIKRDPTKPRAIEIVSEQTNDAVNMEETIYVPVIGKVTAGIPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGESMIEAGILDGDKVIVRSQTIAENGDIIVAMTEDDEATVKRFYKEKTRYRLQPENSTMSPIYLDNVTVIGKVIGLYREL

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.229 kDa
Sequence
MRELTKRQNEIFEYIKQTVHAKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVTEQLGEPINMEETIHVPVIGKVTAGIPITAVENVEEYFPLPEHFTSTHNSDIFILNVVGNSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEENEATVKRFFKEKAHYRLQPENSSMDPIYLDQVTVLGKVVGLFREM

Gene
lexA
Protein
LexA repressor
Organism
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.093 kDa
Sequence
MTKLSKRQQMIFDFIKSEVKLKGYPPSVREIAVAVGLASSSTVHGHLERLENKGYIRRDPTKPRAIEIIDLEMEQQLPKDEARYAPVIGKVTAGIPITAVENIEEFVPIPSSSAGPDDNVFVLVIDGESMIEAGILDGDMVIVKQQNTAVNGEIVVAMTEENEATVKRFFKEENRIRLQPENATMEPLFYDNVTILGKVIGLYRNIH

Gene
lexA
Protein
LexA repressor
Organism
Marinomonas sp. (strain MWYL1)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.574 kDa
Sequence
MIKLTKRQSDVLETIREFISETGFPPTRAEIARRLGFKSPNAAEEHLKALCKKGAIEMLSGASRGIRLVDRASNDDPTDNLGLPVIGKVAAGYPILAQENIASHVNIPANMFSPQADYFLSVSGTSMKDIGIMEGDLLAVHKTTTVRNGQIVVARIGDEVTVKRFEQKGSIVRLIPENEEFNDIIVDLESEEFAIEGLSVGVIRQGL

Gene
lexA
Protein
LexA repressor
Organism
Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.879 kDa
Sequence
MKDLTAKQRSVLIFIEEFIEKNGYPPSVREIARRFRITPRGAQLHLVALEKKGYIERKNGKPRAMRVTKSVKNRVPLIGEIRAGEKKEAIEYLEDYIEVPGSFLSSGYEHFLLRVKGESMIEEHICDGDLVLIRRQDWAQNGDIVAAMVEGEVTLKKFFQRGEMVELRPANKEMSPMFFRADRVKILGKVVGVFRKYEGGRTCFLTR

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.332 kDa
Sequence
MRELTKRQSEIYNYIKQVVQMKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain USA300)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.301 kDa
Sequence
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.301 kDa
Sequence
MRELTKRQSEIYNYIKQVVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSDQTNDNINMEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGDSMIEAGILDGDKVIVRSQTIAENGDIIVAMTEEDEATVKRFYKEKNRYRLQPENSTMEPIYLDNVAVIGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / JCM 1131 / NCIMB 11718 / AM63)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.048 kDa
Sequence
MTEPHANKQLEILRFIYDTVEERAFPPTVREICSAVDLSSTSTVHGHLARLEKKGYILKDATKPRAIEVTEKGREALGIKPKDIPIVGVVTAGQPILAVQDIDEYFPLPPDLENDAGELFMLRVHGESMINAGILNGDHVIVRKQSSANNGEIVVAMTEDNEATVKRFFKEDGYYRLQPENDTMDPIILPVVQILGKVVGLYRNNID

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.034 kDa
Sequence
MTEPHANKQLEILRFIYDTVEERAFPPTVREICSAVDLSSTSTVHGHLARLEKKGYILKDATKPRAIEVTEKGREALGIKPKDIPVVGVVTAGQPILAVQDIDEYFPLPPDLENDAGELFMLRVHGESMINAGILNGDHVIVRKQSSANNGEIVVAMTEDNEATVKRFFKEDGYYRLQPENDTMDPIILPVVQILGKVVGLYRNNID

Gene
lexA
Protein
LexA repressor
Organism
Vibrio vulnificus (strain CMCP6)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.994 kDa
Sequence
MKPLTPRQQQVFDLIKSKIEVTGMPPTRAEIARELGFRSANAAEEHLKALARKQVIEIVPGASRGIRILLEEEAANDEPGLPLIGRVAAGEPILAQEHVEMHYQVDPSMFRPQADFLLRVHGESMKDIGIMDGDLLAVHKTQDVRNGQVVVARVEDDVTVKRLERKGSTVLLHAENEEFAPIEVDLTSQQLTIEGIAVGIIRNTDWM

Gene
lexA
Protein
LexA repressor
Organism
Vibrio vulnificus (strain YJ016)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.994 kDa
Sequence
MKPLTPRQQQVFDLIKSKIEVTGMPPTRAEIARELGFRSANAAEEHLKALARKQVIEIVPGASRGIRILLEEEAANDEPGLPLIGRVAAGEPILAQEHVEMHYQVDPSMFRPQADFLLRVHGESMKDIGIMDGDLLAVHKTQDVRNGQVVVARVEDDVTVKRLERKGSTVLLHAENEEFAPIEVDLTSQQLTIEGIAVGIIRNTDWM

Gene
lexA
Protein
LexA repressor
Organism
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.908 kDa
Sequence
MKPLTPRQAEVLELIKANMNETGMPPTRAEIAQKLGFKSANAAEEHLKALAKKGVIEIMPGTSRGIRLLLEEEEPLEESGLPLIGKVAAGEPILAQEHIESHYQVDPALFHPRADFLLRVQGMSMKNIGILDGDLLAVHKTQEVRNGQVVVARLDEDVTVKRFQRKGSQVWLLPENEELSPIEVDLSCQQLTIEGLAVGVIRNADWM

Gene
lexA
Protein
LexA repressor
Organism
Aeromonas salmonicida (strain A449)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.852 kDa
Sequence
MKPLTPRQAEVLELIKVNMSETGMPPTRAEIAQKLGFKSANAAEEHLKALAKKGVIEIMPGTSRGIRLLIEEEAVLEETGLPLIGKVAAGEPILAQEHIESHYQVDPALFHPRADFLLRVQGMSMKNIGILDGDLLAVHKTQEVRNGQVVVARLDEDVTVKRFQRKGSQVWLLPENEELEPIAVDLSCQQLTIEGLAVGVIRNADWM

Gene
lexA
Protein
LexA repressor
Organism
Aliivibrio salmonicida (strain LFI1238)
Length
207 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.854 kDa
Sequence
MKPLTARQQEVFELIKAKIEDTGMPPTRAEIARELGFRSANAAEEHLKALARKQAIEIIPGASRGIRILLQDPVEPEDLGLPLIGQVAAGEPILAQEHVESHYQVDPSMFKPQADFLLRVNGESMKNIGIMDGDLLAVHKTQDVHDGQVVVARVDDDVTVKRLERKGSMVFLHAENEEFAPIQVDLTSQHLSIEGIAVGVIRSTTWM

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.672 kDa
Sequence
MATHDSKQLEILQYIYDTVENRGFPPTVREICAAVGLSSTSTVHGHLTRLERKGYLIKDATKPRALEITHAGLDALGIKPKDIPVIGVVTAGQPILAVQDVEDYFPLPPNLASDAGELFMLRVHGTSMINAGILNGDYVIVRKQTTAQNGEIVVAMTDDGEATVKRFFKEDLHYRLQPENDAMDPIILNHVQILGKVVGLYRTNID

Gene
lexA
Protein
LexA repressor
Organism
Shewanella baltica (strain OS223)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.635 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLTAEVEEVTETGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPAADFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNVVYLHAENEDYSPIKVDLGYQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella baltica (strain OS155 / ATCC BAA-1091)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.635 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLTAEVEEVTETGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPAADFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNVVYLHAENEDYSPIKVDLGYQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella baltica (strain OS185)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.635 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLTAEVEEVTETGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPAADFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNVVYLHAENEDYSPIKVDLGYQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella baltica (strain OS195)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.635 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLTAEVEEVTETGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPAADFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNVVYLHAENEDYSPIKVDLGYQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella halifaxensis (strain HAW-EB4)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.719 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIARRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIKLTQENTEDADLGLPLIGQVAAGEPILAQEHVEQHYKVDPAMFKPSADFLLRVRGDSMKNIGILEGDLLAVHKIQQARNGQIVVARVEDDVTVKRFEKKGNKVFLHAENEEYSPIEVDLANQSLSIEGLAVGVIRNGDWQ

Gene
lexA
Protein
LexA repressor
Organism
Shewanella oneidensis (strain MR-1)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.747 kDa
Sequence
MRPLTPRQAEILELIKRNIAETGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLPVEEEDNSETGLPLIGQVAAGEPILAQEHVEQYYQIDPSMFHPTANFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNVVYLHAENEDYSPIKVDLSFQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.747 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIARRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIKLTQESTEEPDLGLPLIGQVAAGEPILAQEHVEQHYKVDPAMFRPSADFLLRVRGDSMKNIGILEGDLLAVHKIEQARNGQIVVARVEDDVTVKRFEKKGNKVFLHAENEDYSPIEVDLANQSLSIEGLAVGVIRNGDWQ

Gene
lexA
Protein
LexA repressor
Organism
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.731 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLPAEEEVVVEYGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPTADFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNLVYLYAENEDYSPIKVDLSCQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella piezotolerans (strain WP3 / JCM 13877)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.801 kDa
Sequence
MRPLTPRQAEILELIKRNISDTGMPPTRAEIARRLGFKSANAAEEHLKALAKKGCIEIIPGTSRGIRLTQEEPEEVELGLPLIGQVAAGEPILAQEHVEQHYKVDPAMFRPSADFLLRVRGDSMKDIGILEGDLLAVHKSQQARNGQVVVARVEDDVTVKRFEKKGNKVFLHAENEEYSPIEVDLANQSLSIEGLAVGVIRNGDWQ

Gene
lexA
Protein
LexA repressor
Organism
Bacillus thuringiensis (strain Al Hakam)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus anthracis
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus cereus (strain AH820)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.789 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEERIEISTQSVVQVPIVGKVTAGLPITAVESVEEHFPLPASIIAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQHSANNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILNTVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus cereus (strain Q1)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus cereus (strain ZK / E33L)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.89 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGEDRMDTETQSVIQVPIVGKVTAGLPITAVESVEEHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus pumilus (strain SAFR-032)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.941 kDa
Sequence
MTKLSKRQLDILTFIKEEVKSKGYPPSVREIGEAVGLASSSTVHGHLARLETKGLIRRDPTKPRAIEVLDEEELNIPKSAVMNVPVIGKVTAGLPITAVENVEEYFPLPETFAAPDEQVFMLEIMGESMIDAGILDKDYVIVRQQSTANNGDIVVAMTEEDEATVKRFYKEDTHFRLQPENPSMEPIILQNVSILGKVIGVFRNIH

Gene
lexA
Protein
LexA repressor
Organism
Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.85 kDa
Sequence
MKKMSARQQQILDFIKDEVRAKGYPPSVREIGEAVGLASSSTVHGHLDRLEKRGLIRRDKTKPRAIEILTDDMPTMEEQESVMYVPVIGKVTAGTPITAIENVEEHFPLPAHIVGSDNVYMLSVSGDSMINAGILDGDRVLVRQQSTADNGEIVVAMTEEGEATVKRIYKEASKVRLQPENDELEAMYFDNVSILGKVIGVYRTIH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.077 kDa
Sequence
MTKLSKRQLDILRFIKEEVKTKGYPPSVREIGEAVGLASSSTVHGHLARLETKGLIRRDPTKPRAIEVLDEEEVQIPKSQVVNVPVIGKVTAGIPITAVENIDEYFPLPDRMVPPGEHVFMLEIMGESMIDAGIFDKDYVIVKQQNTANNGEIVVAMTEDDEATVKRFYKEDNYVRLQPENPTMEPIILQNVSILGKVIGVFRTVH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.077 kDa
Sequence
MTKLSKRQLDILRFIKEEVKTKGYPPSVREIGEAVGLASSSTVHGHLARLETKGLIRRDPTKPRAIEVLDEEEVQIPKSQVVNVPVIGKVTAGIPITAVENIDEYFPLPDRMVPPGEHVFMLEIMGESMIDAGIFDKDYVIVKQQNTANNGEIVVAMTEDDEATVKRFYKEDNYVRLQPENPTMEPIILQNVSILGKVIGVFRTVH

Gene
lexA
Protein
LexA repressor
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.239 kDa
Sequence
MRELTKRQSEIYDYIKKIVQTKGYPPSVREIGEAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEIVSEQLDEVNVEETIHVPVIGKVTAGVPITAVENIEEYFPLPEHLTSTHNSDIFILNVVGESMIEAGILDGDKVIVRSQTIAENGDIIVAMTEDEEATVKRFYKEKNRYRLQPENSTMEPIYLDNVIVVGKVIGLYREM

Gene
lexA
Protein
LexA repressor
Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.016 kDa
Sequence
MNLTPAQERVYGFVRDYIQKNGYSPSYEEIRQNLGFRSLNAVFKHLKQLEQRGYVQSLWKNKKRALELLPLHTGAVSIPFLGVVAAGTPIEAVEIPESVEVPESFLANGNNFALRVKGDSMIEEGIREGDILIVARQSRAENGQTVVALVQGEATVKKFYQRGEEIELRPANSRMQPIHARADAVEVVGTVVGLLRNYRRRSLGVV

Gene
lexA
Protein
LexA repressor
Organism
Tolumonas auensis (strain DSM 9187 / TA4)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.581 kDa
Sequence
MKQLTPRQAEVLALIRSAVQQTGMPPTRAEIASELGFKSANAAEEHLKALARKGVIRMMPGTSRGIQLLTDEPEEDEGLPLIGRVAAGEPILAQQHIETHYQIDGSLFHPRADFLLRVHGMSMKNIGILDGDLLAVHKTTQANNGQVVVARVGDDEVTVKRFERKGHIVQLLPENEELQPIVVDLTQENLSIEGLAVGVIRNGNWL

Gene
lexA
Protein
LexA repressor
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.742 kDa
Sequence
MKPLTPRQQQVFDLIKSKIEDTGMPPTRAEIARELGFRSANAAEEHLKALARKQAIEIIPGASRGIRILLEDAANDDQGLPLIGQVAAGEPILAQEHVESHYQVDPAMFKPKADFLLRVNGESMKDIGIMDGDLLAVHKTQDVRDGQVVVARVDDDVTVKRLERKGSTVLLHAENEEFSPIQVDLTSQHLTIEGLAVGIIRNTDWM

Gene
lexA
Protein
LexA repressor
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.71 kDa
Sequence
MKPLTPRQQQVFDLIKSKIDDTGMPPTRAEIARELGFRSANAAEEHLKALARKQAIEIIPGASRGIRILLEDAANDEQGLPLIGQVAAGEPILAQEHVEAHYQVDPAMFKPQADFLLRVNGESMKDIGIMDGDLLAVHKTQDVRDGQVVVARVDDDVTVKRLERKGSTVLLHAENEEFAPIQVDLTSQHLTIEGLAVGIIRNTDWM

Gene
lexA
Protein
LexA repressor
Organism
Vibrio tasmaniensis (strain LGP32)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.826 kDa
Sequence
MKPLTPRQQQVFDLIKSKIEDCGMPPTRAEIARELGFRSANAAEEHLKALARKEAIEIIPGASRGIRILLEDAANEEQGLPLIGQVAAGEPILAQEHVEMHYQVDPGMFKPQADFLLRVNGESMKDIGIMDGDLLAVHKTQDVRDGQVVVARVDDDVTVKRLERKGSTVLLHAENEEFSPIHVDLESQHLSIEGLAVGIIRNTDWM

Gene
lexA
Protein
LexA repressor
Organism
Shewanella sp. (strain ANA-3)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.731 kDa
Sequence
MRPLTPRQAEILELIKRNIAETGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLPVEEEDNSESGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPAANFLLRVRGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNLVYLHAENEDYSPIKVDLSFQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella sediminis (strain HAW-EB3)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.636 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIAKRLGFKSANAAEEHLKALAKKGCIEIIPGTSRGIRLTQANESEEELGLPLIGQVAAGEPILAQEHVEQHYQIDPAMFRPSADFLLRVRGDSMKNIGILEGDLLAVHKAEQARNGQVVVARVEDDVTVKRFEKKGSIVYLHAENEDYSPIVVDLTSESLSIEGLAVGVIRNGDWQ

Gene
lexA
Protein
LexA repressor
Organism
Shewanella sp. (strain MR-4)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.732 kDa
Sequence
MRPLTPRQAEILELIKRNIAETGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLPVEEEDNSESGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPAADFLLRVRGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNLVYLHAENEDYSPIKVDLSFQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella sp. (strain MR-7)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.734 kDa
Sequence
MRPLTPRQAEILELIKRNIAETGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLPVEEEDNSETGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPSADFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNLVYLHAENEDYSPIKVDLSFQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella sp. (strain W3-18-1)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.731 kDa
Sequence
MRPLTPRQAEILELIKRNIADTGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLPAEEEVVVEYGLPLIGQVAAGEPILAQEHVEQYYQVDPSMFHPTADFLLRVKGDSMKNIGILEGDLLAVHKVQQARNGQVVVARVDDDVTVKRFEKKGNLVYLYAENEDYSPIKVDLSCQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.672 kDa
Sequence
MATHDSKQLEILQYIYDTVENRGFPPTVREICAAVGLSSTSTVHGHLTRLERKGYLIKDATKPRALEITHAGLDALGIKPKDIPVIGVVTAGQPILAVQDVEDYFPLPPNLASDAGELFMLRVHGTSMINAGILNGDYVIVRKQTTAQNGEIVVAMTDDGEATVKRFFKEDLHYRLQPENDAMDPIILNHVQILGKVVGLYRTNID

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus salivarius (strain UCC118)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.998 kDa
Sequence
MTKSEKRQHDILRYIFSHVSDSGYPPTVREICNAVGLSSTSTVHGHLSKLESKGLIKRDPTKPRAIEITLAGLEMLDELPNKTQIPIVGTVTAGEPILAVEENRDYFPLPPYFESADDLFMLSIRGESMINAGILDGDQVIVRKQSSANNGEIVIAMTEENEATCKRFFKEDGYYRLQPENDTMDPIILENVTILGKVVGLYRDLI

Gene
lexA
Protein
LexA repressor
Organism
Alkaliphilus metalliredigens (strain QYMF)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.048 kDa
Sequence
MYEDLNDNQIKILHYMKSEISQKGYPPSVREICQAVGLKSTSTAHGHLSKLELKGYIRRDATKPRAIEILSQGDEQSPYIHKEIINVPIVGKVTAGQPILAVENIEDTFPLPIDFVDSESTFILTVKGDSMIDDGIHENDYVVVRQQSDARNGDIVVALIDDSATVKRFYREKDHIRLQPSNTSMSPILVDDVTILGKVTGVFRKI

Gene
lexA
Protein
LexA repressor
Organism
Alkaliphilus oremlandii (strain OhILAs)
Length
206 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.177 kDa
Sequence
MYEDLNGKQLEILNYMKMEINKRGYPPSVREICEAVGLRSTSTVHGHLAKLEDKGYIRRDPTKPRAIEILSNDPFSDYSHNKEMVQVPIVGKVTAGQPILATENIEDTFPLPLNFIDHGNTFILNVKGESMIEAGILDNDYVVIRQQSTASNGDIVVALIDDEATVKRFFKESDHIRLQPENSLMDPILLKDVVILGKVIGVFRKL

Gene
lexA
Protein
LexA repressor
Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.393 kDa
Sequence
MRPLTPRQSEILELIKDNLHATGMPPTRAEIAHKLGFRSANSAEEHLKALARKGVIEILPGMSRGIRLVGDDYDIADGLPLIGQVAAGEPLLAEQHVEGHYKIDESLFHPAASFLLKVNGMSMRDIGILDGDLLAVHKTEQARNGQIVVARVEDEVTVKRFEQRGKTILLHPENEDFSTITVNLAEQVFAIEGLAVGVIRNGATL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.6 kDa
Sequence
MRPLTPRQTEILELIKRNIADTGMPPTRAEIATRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIRLTQEDAEVELGLPLIGQVAAGEPILAQEHVEQYFQVDPHMFKPAANFLLRVRGDSMKNIGILEGDLLAVHKMQEAKNGQVVVARVEDDVTVKRFEKKGNVIYLHAENEDYAPIKVDLTCQSLTIEGLAVGVIRNGAWL

Gene
lexA
Protein
LexA repressor
Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.668 kDa
Sequence
MRPLTPRQAEILDLIKRNIADTGMPPTRAEIARRLGFKSANAAEEHLKALAKKGCIEIMPGTSRGIKLTQEEEPEDLGLPLIGQVAAGEPILAQEHVEQHYQVDPSMFRPSADFLLRVRGDSMKDIGILEGDLLAVHKVEQARNGQIVVARVEDDVTVKRFEKRGSTVYLHAENEEYSPIVVDLTTQSLSIEGLAVGVIRNGDWQ

Gene
lexA
Protein
LexA repressor
Organism
Bacillus subtilis (strain 168)
Length
205 amino acids
Function
Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative (PubMed:1657879, PubMed:8969214, PubMed:9555905). In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA (PubMed:8969214).
Similarity
Belongs to the peptidase S24 family.
Mass
22.849 kDa
Sequence
MTKLSKRQLDILRFIKAEVKSKGYPPSVREIGEAVGLASSSTVHGHLARLETKGLIRRDPTKPRAIEILDEEVDIPQSQVVNVPVIGKVTAGSPITAVENIEEYFPLPDRMVPPDEHVFMLEIMGDSMIDAGILDKDYVIVKQQNTANNGEIVVAMTEDDEATVKRFYKEDTHIRLQPENPTMEPIILQNVSILGKVIGVFRTVH

Gene
lexA
Protein
LexA repressor
Organism
Petrotoga mobilis (strain DSM 10674 / SJ95)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.336 kDa
Sequence
MEELTKRQSQVLDFIKSYMEKNGFAPSIRDIMKHFNFKSPRAAHKHLIILEKKGYIERKNVSRGIKMMPKSGEIFATETLAPVSGKIAAGDAIEAIQTISDYIPIPTNFFPKNYEYFSLRVEGNSMIEAQIKSGDFVLIRKQDYAMDGDIVVALIDGNDATLKRYKRLNEDEVLLIPENKSMKEIKVKADHLKIQGKMVGLIRVL

Gene
lexA
Protein
LexA repressor
Organism
Providencia rettgeri
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.847 kDa
Sequence
MKALTARQQQVYDLVRDHISQTGMPPTRAEIAASLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLLEEETEDQGLPLIGRVAAGEPLLAQEHIESHYQVDPELFKPHADFLLRVNGMSMKDIGIMDGDLLAVHKTQNVHNGQVVVARIEDEVTVKRFKQQGNRVELIAENPEFEPIVVDLRQQNFTIEGLAVGVIRNSDWY

Gene
lexA
Protein
LexA repressor
Organism
Bacillus subtilis (strain 168)
Length
205 amino acids
Function
Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative (PubMed:1657879, PubMed:8969214, PubMed:9555905). In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA (PubMed:8969214).
Similarity
Belongs to the peptidase S24 family.
Mass
22.849 kDa
Sequence
MTKLSKRQLDILRFIKAEVKSKGYPPSVREIGEAVGLASSSTVHGHLARLETKGLIRRDPTKPRAIEILDEEVDIPQSQVVNVPVIGKVTAGSPITAVENIEEYFPLPDRMVPPDEHVFMLEIMGDSMIDAGILDKDYVIVKQQNTANNGEIVVAMTEDDEATVKRFYKEDTHIRLQPENPTMEPIILQNVSILGKVIGVFRTVH

Gene
lexA
Protein
LexA repressor
Organism
Petrotoga mobilis (strain DSM 10674 / SJ95)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.336 kDa
Sequence
MEELTKRQSQVLDFIKSYMEKNGFAPSIRDIMKHFNFKSPRAAHKHLIILEKKGYIERKNVSRGIKMMPKSGEIFATETLAPVSGKIAAGDAIEAIQTISDYIPIPTNFFPKNYEYFSLRVEGNSMIEAQIKSGDFVLIRKQDYAMDGDIVVALIDGNDATLKRYKRLNEDEVLLIPENKSMKEIKVKADHLKIQGKMVGLIRVL

Gene
lexA
Protein
LexA repressor
Organism
Providencia rettgeri
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.847 kDa
Sequence
MKALTARQQQVYDLVRDHISQTGMPPTRAEIAASLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLLEEETEDQGLPLIGRVAAGEPLLAQEHIESHYQVDPELFKPHADFLLRVNGMSMKDIGIMDGDLLAVHKTQNVHNGQVVVARIEDEVTVKRFKQQGNRVELIAENPEFEPIVVDLRQQNFTIEGLAVGVIRNSDWY

Gene
lexA
Protein
LexA repressor
Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.097 kDa
Sequence
MPEPLTERQRQILQFIKDEIRTKGYPPSVREIGEAIGLSSSSTVHGHMTRLEEKGYIRRDPTKPRAIEVLDGSHTQLKRTIAVPVVGRVTAGQPILAQESIEDHFPLPADFVRADESELFFLTVQGDSMIEAGILDGDYVLVHRQQHANNGDIVVALIEDEATVKRFFKEQDHIRLQPENRFMDPIIVPDCQILGKVVGLVRRMG

Gene
lexA
Protein
LexA repressor
Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.626 kDa
Sequence
MDELTPRQSEILAWIRARMAEDSLPPTRAELMRAFDFRSPNAAESHLRVLARKGYILLQSGTARGIRLCASEEETGLPLIGRVAAGQPMLAEEFREGQLPVDPKLFSPGADYLLRVQGMSMRDAGILDGDILAVRHDASLTLQDGQMVVARVNGEVTVKRWKRDGKQVWLLPENPDFSPISVDLQRDSLTIEGVVVGLLRIGGNL

Gene
lexA
Protein
LexA repressor
Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.626 kDa
Sequence
MDELTPRQSEILAWIRARMAEDSLPPTRAELMRAFDFRSPNAAESHLRVLARKGYILLQSGTARGIRLCASEEETGLPLIGRVAAGQPMLAEEFREGQLPVDPKLFSPGADYLLRVQGMSMRDAGILDGDILAVRHDASLTLQDGQMVVARVNGEVTVKRWKRDGKQVWLLPENPDFSPISVDLQRDSLTIEGVVVGLLRIGGNL

Gene
lexA
Protein
LexA repressor
Organism
Lysinibacillus sphaericus (strain C3-41)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.804 kDa
Sequence
MKKVSKRQEDILAFIKDEVRAKGYPPSVREIGEAVGLASSSTVHGHLARLEQKGFIRRDPTKPRAIEILEPEESIQKQHVIHVPLVGKVTAGSPITAIENIEEYFPLPDTYGTSEDQLFMLEIMGESMIEAGILDGDLVIVKQKSTANNGDIVVAMTAEDEATVKRFFKEKNHFRLQPENSSMEPIIVDQVSIGGQVVGLYRRVH

Gene
lexA
Protein
LexA repressor
Organism
Shewanella woodyi (strain ATCC 51908 / MS32)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.549 kDa
Sequence
MRPLTPRQAEILELIKCNIAETGMPPTRAEIAKRLGFKSANAAEEHLKALAKKGCIEIIPGTSRGIRLAQTEELEEQGLPLIGQVAAGEPILAQEHVEQHYQVDPNMFHPSADFLLRVRGDSMKDIGILEGDLLAVHKAEQARNGQVVVARVEDDVTVKRFEKKGSTVYLHAENEDYSPIVVDLTNQSLSIEGLAVGVIRNGDWQ

Gene
lexA
Protein
LexA repressor
Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Length
205 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.832 kDa
Sequence
MQPDLSPQLAMVLNYIRHFIDINGYPPSIRDICKATGLRSSSTVYNYLNKLEEKGYIRRDPSRSRAIEILTPYPALTRAKNMVSVPLLGKITAGQPILAFENIEDVFPLPADLAGAENAFMLHVSGDSMIEAGILDGDYLIVRPQDTAENGDIVVALLEDEATVKYFYRYPDHIELVPANSSMQPLIVHKVTILGKVVGLYRHFS

Gene
lexA
Protein
LexA repressor
Organism
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.824 kDa
Sequence
MKNSLLSHQEKKIISFIKQYLNENGYPPTIREICQGVGLSSPSTVHHHLKNLESKGYLQRNPTKPRALELVAEKAPEELLSIPLLGNVAAGYPTLAIENAEEEMQIPKSLFPEKELFALRIKGDSMIEEGILPGDVIIVKKQEVAENGDIVVAYLEGEVTVKKFWKDSVNGVIKLIPANSKYEPIIINRETKILGKVIGLLRRY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.066 kDa
Sequence
MATDKITRDVQSEIYEFIRQEVLDKGYPPSVREICAKVGLSSTSTVHGHLSRLEKKGLIRRDPTKPRAIELIKDPISKREMIDIPIVGKVQAGQPILAVENIDDYLTIPLNFVRNTNDLFILKISGNSMIEAGIYDGDLAIIEKTNYAQNGDIVVALIENDATIKRFFKEKDKIRLQPENHTMDPIIVDNCEVIGKLAGIYRRY

Gene
lexA
Protein
LexA repressor
Organism
Shewanella frigidimarina (strain NCIMB 400)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.591 kDa
Sequence
MRPLTPRQAEILDLIKNNIAETGMPPTRAEIANRLGFKSANAAEEHLKALAKKGFIEIMPGTSRGIRLPQEEQVETGLPLIGQVAAGEPILAQEHVEQYYQVDPNMFKPAADFLLRVRGDSMKNIGILEGDLLAVHKMQQARNGQVVVARVDDDVTVKRFEQKGNVIYLHAENEDYNPIKVDLSCQSLTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.939 kDa
Sequence
MRKMSKRQQEILDYIVAQVKLKGYPPSVREIGEAVGLASSSTVHGHLDRLEKRGLIRRDPTKPRAIEILLDKPEEDHEAIVHIPVIGKVTAGFPITAIENIEEHFPLPAHYVGNENVFMLTIDGESMINAGILDGDRVIVRQQNTAENGEIVVAMTEDSEATVKRFFLEDQQVRLQPENDSMDPMYFDNVSILGKVIGVYRTIH

Gene
lexA
Protein
LexA repressor
Organism
Bacillus weihenstephanensis (strain KBAB4)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.629 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGDNRTETQSVIQVPIIGKVTAGLPITAVESVEDHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain PA7)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.522 kDa
Sequence
MQKLTPRQSEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARLGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.506 kDa
Sequence
MQKLTPRQAEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARIGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.506 kDa
Sequence
MQKLTPRQAEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARIGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.506 kDa
Sequence
MQKLTPRQAEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARIGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Bacillus weihenstephanensis (strain KBAB4)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.629 kDa
Sequence
MEKLTKRQQDILDFIKLKVQEKGYPPSVREIGQAVGLASSSTVHGHLSRLEEKGYIRRDPTKPRAIEILGDNRTETQSVIQVPIIGKVTAGLPITAVESVEDHFPLPASIVAGADQVFMLRISGDSMIEAGIFDGDLVVVRQQQSAYNGEIVVALTEDNEATVKRFYKEKDHFRLQPENSSLEPIILKQVSVIGKVIGVYRDLH

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain PA7)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.522 kDa
Sequence
MQKLTPRQSEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARLGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.506 kDa
Sequence
MQKLTPRQAEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARIGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.506 kDa
Sequence
MQKLTPRQAEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARIGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.506 kDa
Sequence
MQKLTPRQAEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARIGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.997 kDa
Sequence
MYPDLSQRQTDILEYIKRVIREKGYPPSVREIGDAVGLMSSSTVHGHLQTIEEKGYIRRDPTKPRAIEILDSSSDANEKKTVFVPIIGKVTAGQPILAQENIEDTFPLPVDVVNSDTVFMLRVKGESMIDAGIMDGDLILVRQQKVARNGEIVVAMIDEEATVKRFYKEKTLIRLQPENPYMEPIYSQDVTILGKVIGVFRILH

Gene
lexA
Protein
LexA repressor
Organism
Desulfitobacterium hafniense (strain Y51)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.997 kDa
Sequence
MYPDLSQRQTDILEYIKRVIREKGYPPSVREIGDAVGLMSSSTVHGHLQTIEEKGYIRRDPTKPRAIEILDSSSDANEKKTVFVPIIGKVTAGQPILAQENIEDTFPLPVDVVNSDTVFMLRVKGESMIDAGIMDGDLILVRQQKVARNGEIVVAMIDEEATVKRFYKEKTLIRLQPENPYMEPIYSQDVTILGKVIGVFRILH

Gene
lexA
Protein
LexA repressor
Organism
Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.477 kDa
Sequence
MNNELKLGKRQKQILDFIKQSCKEKGYPPSVREIGQAVGLKSSSTVHTHLVRLEEKGLIRRDPAKPRAIIPLDDEPLLQSEALSVPVIGNVAAGSPILAEQNIDNYLSIPVDFLGSGNHFILKVKGDSMIEAGILDGDYLIVREQADASNGEIVVALLDNEATVKRFYRRDDYVELRPENALMDPITVNNVQVAGKVAGLLRRI

Gene
lexA
Protein
LexA repressor
Organism
Clostridium novyi (strain NT)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.816 kDa
Sequence
MSRSSEDKQIEIYEFIKEQIIEKGYPPSVREICKGVGLSSTSSVHGHLSKLEKKGLIRRDSTKPRTIEILKEPIVPKEMVNIPILGKVTAGTPILAVENIEDTFPISLNFIPSNKDLFMLKISGESMIDAGILDGDLAIIEKTNTAKNGEIVVALIDNEVTLKRFFKEDKHIRLQPENKNMDPIILEDDSVSIVGKLAGIFRRY

Gene
lexA
Protein
LexA repressor
Organism
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.632 kDa
Sequence
MKISKRQQDIYEFIKSEVKEKGYPPSVREIGEAVGLASSSTVHGHLARLEGKGLIRRDPTKPRAIEILSLEDEAETPNVVNIPIIGKVTAGMPITAIENIEEYFPLPEYMAAGETNVFMLEIDGESMINAGILDGDKVIVRQQSSAINGEIVVAMTDENEATCKRFYKEANHFRLQPENDALEPIILNNVTILGKVIGLYRDIH

Gene
lexA
Protein
LexA repressor
Organism
Listeria monocytogenes serotype 4b (strain CLIP80459)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.637 kDa
Sequence
MKISKRQQDIYEFIKSEVKEKGYPPSVREIGEAVGLASSSTVHGHLARLEGKGLIRRDPTKPRAIEILSLEDEAETPNVVNIPIIGKVTAGMPITAIENIDEYFPLPEYMAAGETNVFMLEIDGESMINAGILDGDKVIVRQQSSAINGEIVVAMTDENEATCKRFYKEANHFRLQPENDALEPILLNNVTILGKVIGLYRDIR

Gene
lexA
Protein
LexA repressor
Organism
Listeria monocytogenes serotype 4b (strain F2365)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.637 kDa
Sequence
MKISKRQQDIYEFIKSEVKEKGYPPSVREIGEAVGLASSSTVHGHLARLEGKGLIRRDPTKPRAIEILSLEDEAETPNVVNIPIIGKVTAGMPITAIENIDEYFPLPEYMAAGETNVFMLEIDGESMINAGILDGDKVIVRQQSSAINGEIVVAMTDENEATCKRFYKEANHFRLQPENDALEPILLNNVTILGKVIGLYRDIR

Gene
lexA
Protein
LexA repressor
Organism
Listeria monocytogenes serotype 4a (strain HCC23)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.637 kDa
Sequence
MKISKRQQDIYEFIKSEVKEKGYPPSVREIGEAVGLASSSTVHGHLARLEGKGLIRRDPTKPRAIEILSLEDEAETPNVVNIPIIGKVTAGMPITAIENIDEYFPLPEYMAAGETNVFMLEIDGESMINAGILDGDKVIVRQQSSAINGEIVVAMTDENEATCKRFYKEANHFRLQPENDALEPILLNNVTILGKVIGLYRDIR

Gene
lexA
Protein
LexA repressor
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.638 kDa
Sequence
MKISKRQQDIYEFIKSEVKEKGYPPSVREIGEAVGLASSSTVHGHLARLEGKGLIRRDPTKPRAIEILSLEDEAETPNVVNIPIIGKVTAGMPITAIENIDEYFPLPEYMAAGETNVFMLEIDGESMINAGILDGDKVIVRQESSAINGEIVVAMTDENEATCKRFYKEANHFRLQPENDALEPILLNNVTILGKVIGLYRDIR

Gene
lexA
Protein
LexA repressor
Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.678 kDa
Sequence
MKISKRQQDIYEFIKSEVKEKGYPPSVREIGEAVGLASSSTVHGHLARLEGKGLIRRDPTKPRAIEILSLEDEAETPNVVNIPIIGKVTAGMPITAIENIEEYFPLPEYMAAGETNVFMLEIDGESMINAGILDGDKVIVRQQNSAINGEIVVAMTDENEATCKRFYKEANHFRLQPENDALEPIILNNVTILGKVIGLYRDIR

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas mendocina (strain ymp)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.47 kDa
Sequence
MLKLTPRQAEILAFIKRCLEDNGYPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPGAANEDEGLPVIGRVAAGAPILAQQHVEESCQINPAFFHPKADYLLRVRGMSMKDIGIFDGDLLAVHTTREARNGQIVVARLDDEVTVKRFKREGNKVWLIAENPEFAPIEVDLEQQDLVIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Lactobacillus sakei subsp. sakei (strain 23K)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.568 kDa
Sequence
MTKTESKQLEVLRFIHERVQDKGYPPTVREICEAVNLSSTSTVHGHLARLEKKGLLQKDPTKPRAIELTPAGLTAIGATPQKIPVLGVVTAGVPILAVEEATDYFPLPPSLQTEQDLFMLTIRGESMINAGILDGDEVIIRKQSTADNGDIVIAMTAEDEATCKRFFKEADHYRLQPENDTFEPIILNEVSILGKVVGLYRDRM

Gene
lexA
Protein
LexA repressor
Organism
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Length
204 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.493 kDa
Sequence
MSSKLTDRQQQVLDCIRECLKDNGMAPTRAEIADIMGFQSKNAASDHLRALERKGYIKLHSDRSRGIQLLDHAYWGEEELPVVGKVAAGIPIEAIENVERTVPVPQGLFKQRPTYLLKVQGDSMVDAGIFDGDLIAVRKSNVARSGEIVVARIDEEVTVKTLKLNKSSATLLPANEAYEPIKVPADQLIIEGIFVGLIRDPNSF

Gene
lexA
Protein
LexA repressor
Organism
Aromatoleum aromaticum (strain EbN1)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.207 kDa
Sequence
MISRADPLTARQAEILDFIRHTVESEGRPPTRAEICTAFGFRSPNAAETHLRTLAAKGAIVLEEGRARGIRLVEALGLPLVGHVAAGRPMLAVEHIEARYQIDSALFSPRADYLLRVRGMSMRDAGIIDSDLLAVHRTPQVRAGQVVVARLEDEVTVKTFTREGPIVRLLPANPDFEPIVVDTRHQALDIEGIAVGLVRNGSR

Gene
lexA
Protein
LexA repressor
Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.567 kDa
Sequence
MTEELTPKQAAVLEFIKKSIRQRGYPPSVREIGQEVGLSSSSTVHGYLKKLEEKGYLRRDATKPRAIEVLDNPAGEKVEFINVPVLGRVAAGVPLLAVENREDIFPLPVHFTGSGEFFMLTVRGDSMIEAGILNGDMVVVRRQQDAGNGDIVVALLEEEATVKRLFKENGRIRLQPENRLMEPIYAAEVQILGKVIGLVRKIY

Gene
lexA
Protein
LexA repressor
Organism
Proteus mirabilis (strain HI4320)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.444 kDa
Sequence
MKALTARQQQVYDLVRDHISQTGMPPTRAEIASQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLLEEEPEGLPLIGRVAAGEPLLAQEHIESHYQVDPMLFKPSADFLLRVNGMSMKDIGIMDGDLLAVHKTQDVHNGQVIVARIEDEVTVKRFKKVGSKIELHAENPEFSPIIVDLREQSFTVEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.567 kDa
Sequence
MTEELTPKQAAVLEFIKKSIRQRGYPPSVREIGQEVGLSSSSTVHGYLKKLEEKGYLRRDATKPRAIEVLDNPAGEKVEFINVPVLGRVAAGVPLLAVENREDIFPLPVHFTGSGEFFMLTVRGDSMIEAGILNGDMVVVRRQQDAGNGDIVVALLEEEATVKRLFKENGRIRLQPENRLMEPIYAAEVQILGKVIGLVRKIY

Gene
lexA
Protein
LexA repressor
Organism
Proteus mirabilis (strain HI4320)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.444 kDa
Sequence
MKALTARQQQVYDLVRDHISQTGMPPTRAEIASQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLLEEEPEGLPLIGRVAAGEPLLAQEHIESHYQVDPMLFKPSADFLLRVNGMSMKDIGIMDGDLLAVHKTQDVHNGQVIVARIEDEVTVKRFKKVGSKIELHAENPEFSPIIVDLREQSFTVEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Desulfatibacillum aliphaticivorans
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.404 kDa
Sequence
MEDLTEKQSLVFEFIMEYTADHGYPPTVRELCDELGFKSPNTAHFHLKGLKDKGYIQSAKGKNRGITVLKTPPGAGGKIPLVGRIAAGAPILAVENVMDTLDVDRAFFGSSDAFSVRVEGDSMIEAHIEDGDYVVIKPTATPRNGDIVAALVNDEVTLKYFHRDGSRIELRPANVRYKPFCYTEEDFIDVRVLGVMAGLIRKV

Gene
lexA
Protein
Transcription regulator LexA
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
203 amino acids
Function
A probable transcription regulator, probably involved in carbon metabolism (PubMed:15225304). Binds and probably regulates expression of bidirectional hydrogenase (hoxEFUHY), probably activates its transcription (PubMed:16102913, PubMed:16238629). A possible regulator of redox-responsive genes. Binds 2 direct repeats of the DNA with sequence 5'-CTA-N(9)-CTA-3' in the upstream region of both its own gene (includes the transcription start site) and crhR (includes the initiation codon) in a sequence-specific manner; does not bind crhR RNA (PubMed:18555801). Binds to the crhR gene, represses its transcription (PubMed:16840531).
Similarity
Belongs to the peptidase S24 family.
Mass
22.744 kDa
Sequence
MEPLTRAQKELFDWLVSYIDETQHAPSIRQMMRAMNLRSPAPIQSRLERLRNKGYVDWTDGKARTLRILHQKPKGVSVIGELKGGELVEADAEEVEKIDFAPLMKKSSVFALRVMSNDLVDDFIVEGDMLILRSVTGEEEIEDGELVAASIKGGKIAIKRYYQDGTKVVLKASNNKGPGQELKASDVEIQGILMGVWRNFQGV

Gene
lexA
Protein
LexA repressor
Organism
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.922 kDa
Sequence
MIIKENSDKQTQIYNFLIEFTKSKGYPPSVREICQAVSLKSTSTVHGHLKRLEKKGLIYRDPTKPRALEIVELSNEEKELIDIPIVGKVTAGMPILATENIEDMFQIPINYVKHNNDLFILKVTGDSMIEAGILDGDLAIIEQKNVATNGDIVVALIENEATIKRFFKENGFIRLQPENKNYEPIIVEDCSILGKLVGIYRAY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium perfringens (strain 13 / Type A)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.94 kDa
Sequence
MIIKENSDKQTQIYNFLIEFTKSKGYPPSVREICQAVSLKSTSTVHGHLKRLEKKGLIYRDPTKPRALEIVELSNEEKELIDIPIVGKVTAGMPILATENIEDMFQMPINYVKHNNDLFILKVTGDSMIEAGILDGDLAIIEQKNVATNGDIVVALIENEATIKRFFKENGFIRLQPENKNYEPIIVEDCSILGKLVGIYRAY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium perfringens (strain SM101 / Type A)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.936 kDa
Sequence
MIIKENSDKQTQIYNFLIEFTKSKGYPPSVREICQAVSLKSTSTVHGHLKRLEKKGLIYRDPTKPRALEIVELSNEEKELIDIPIVGKVTAGMPILATENIEDMFQIPINYVKHNNDLFILKVTGDSMIEAGILDGDLAIIEQKNIATNGDIVVALIENEATIKRFFKENGFIRLQPENKNYEPIIVEDCSILGKLVGIYRAY

Gene
lexA
Protein
LexA repressor
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.604 kDa
Sequence
MKDLTDKQQAVLAFITTIIKERGFPPTIREIGDEFGITAKGAYDHLKAIEKKGYLKTAKNQSRAIELIRQSPMESIPVQATSIPVIGRVAAGLPIFADENIESYIPVPDEMAKGNVPMYALRVQGDSMIEVGIDSGDIAIIEKRDIARNGEIVVALIEDEATLKVYYKEQDQIRLEARNPKYKPIKTKKATVIGKLVGLYRIY

Gene
lexA
Protein
LexA repressor
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.604 kDa
Sequence
MKDLTDKQQAVLAFITTIIKERGFPPTIREIGDEFGITAKGAYDHLKAIEKKGYLKTAKNQSRAIELIRQSPMESIPVQATSIPVIGRVAAGLPIFADENIESYIPVPDEMAKGNVPMYALRVQGDSMIEVGIDSGDIAIIEKRDIARNGEIVVALIEDEATLKVYYKEQDQIRLEARNPKYKPIKTKKATVIGKLVGLYRIY

Gene
lexA
Protein
LexA repressor
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.619 kDa
Sequence
MKDLTDKQQAVLAFITAIIKERGFPPTIREIGDEFGITAKGAYDHLKAIEKKGYLKTAKNQSRAIELIRQSPMESLPVQATSIPVIGQVAAGLPIFAEENIESYIPVPDEMAKGNVPMYALRVQGDSMIEVGINDGDIAIIEKRDIARNGEIVVALIEDEATLKVYYKEQDQIRLEARNPKYKPIKTKKATVMGKLIGLYRIY

Gene
lexA
Protein
LexA repressor
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Length
203 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.619 kDa
Sequence
MKDLTDKQQAVLAFITAIIKERGFPPTIREIGDEFGITAKGAYDHLKAIEKKGYLKTAKNQSRAIELIRQSPMESLPVQATSIPVIGQVAAGLPIFAEENIESYIPVPDEMAKGNVPMYALRVQGDSMIEVGINDGDIAIIEKRDIARNGEIVVALIEDEATLKVYYKEQDQIRLEARNPKYKPIKTKKATVMGKLIGLYRIY

Gene
lexA
Protein
LexA repressor
Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.94 kDa
Sequence
MKKQLTKKQEEILEFIKKRIKEKGYPPAVREICEATGLKSTSTVHGHLTRLEKKGYIRRDPSKPRAIEIVDDDFYVHRNVIRLPLVGKVTAGEPILAVENIEDTITLPYDLVGTEDAFLLRVKGDSMIDAGIFDNDIIIVKRQNVAENGDIVVALIDDEATVKRFFKESDHIRLQPENKAMEPIIVKDVKILGKVIGLIRRM

Gene
lexA
Protein
LexA repressor
Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.344 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLLDEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Klebsiella pneumoniae (strain 342)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.313 kDa
Sequence
MKALTTRQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGAIEIVSGASRGIRLLTEEEHGLPLIGRVAAGEPLLAQQHIEGHYQVDPSMFKPNADFLLRVSGMSMKDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNVVELLPENSEFTPIVVDLRQQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.304 kDa
Sequence
MKALTTRQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGAIEIVSGASRGIRLLTEEEQGLPLIGRVAAGEPLLAQQHIEGHYQVDPSMFKPNADFLLRVSGMSMKDIGILDGDLLAVHKTQDVRNGQVVVARIDEEVTVKRLKKQGNVVELLPENSEFSPIVVDLRQQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella paratyphi C (strain RKS4594)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella typhi
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Serratia proteamaculans (strain 568)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.4 kDa
Sequence
MKALTTRQQEVYDLIRDHISSTGMPPTRAEIAMRLGFRSPNAAEEHLKALARKGVIEIISGASRGIRLLMEDEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPSADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIEDEVTVKRLKKHGNVVELLPENSEFQPIVVDLRQQNFTIEGLAVGVIRNGDWV

Gene
lexA
Protein
LexA repressor
Organism
Azoarcus sp. (strain BH72)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.023 kDa
Sequence
MNARNEQLTSRQQEILDFIRQTVESEGRPPTRAEVCSAFGFKSPNAAETHLRALAAKGAILLEEGRARGIRLAEALGLPLVGRVAAGNPILAAEHVEARIQFDPALFSPRADYLLRVRGMSMRDAGILDGDLIAVHRSHEARNGQVVVARIDDDVTVKTLRRNGPIVELLPANPDFDPIVVDTRSAALELEGIMVGLIRTDH

Gene
lexA
Protein
LexA repressor
Organism
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.458 kDa
Sequence
MHKLTPRQVEILAFIKRCLEENGYPPTRAEIARELGFKSPNAAEEHLKAMARKGAIEMTPGASRGIRIPGSEVESEPTSLPIVGRVAAGAPILAQQHIEETCQIDPGFFHPRADYLLRVRGMSMKDVGIYDGDLLAVHTCREAHNGQIVVARLNDEVTVKRFRRDGDKVWLIAENPEFSPLEIDLTEQDLTIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.413 kDa
Sequence
MKALTVRQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQNFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella agona (strain SL483)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella choleraesuis (strain SC-B67)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella dublin (strain CT_02021853)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella heidelberg (strain SL476)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella newport (strain SL254)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.305 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLQEEEDGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFTPIVVDLREQSFTIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.393 kDa
Sequence
MSPLTPKQKQVFDYIARHIGEQGFAPSQQEIARAFGFRSLGTVRNYLVRLEREGLLERNWNARRGLQLRTASERGMKLPLAGTVAAGKPIEAIEIPDVIEVPPTMVGSGEHFVLRVAGDSMIGDGIIDGDYVVVRKQATAEHGQTVVALLDNEATVKRLHRRNDRIELHPANPSMQPIVVTDPDNFRIEGVVVGVIRHYRSA

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas chlororaphis
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.24 kDa
Sequence
MLKLTPRQAEILAFIKRCLEDNGYPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEAKPDDSSLPIIGRVAAGAPILAEQHIEESCNINPAFFHPRADYLLRVHGMSMKDIGIFDGDLLAVHTTREARNGQVVVARIGDEVTVKRFKREGSKVWLIAENPEFAPIEVNLKDQDLVIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.393 kDa
Sequence
MSPLTPKQKQVFDYIARHIGEQGFAPSQQEIARAFGFRSLGTVRNYLVRLEREGLLERNWNARRGLQLRTASERGMKLPLAGTVAAGKPIEAIEIPDVIEVPPTMVGSGEHFVLRVAGDSMIGDGIIDGDYVVVRKQATAEHGQTVVALLDNEATVKRLHRRNDRIELHPANPSMQPIVVTDPDNFRIEGVVVGVIRHYRSA

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas chlororaphis
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.24 kDa
Sequence
MLKLTPRQAEILAFIKRCLEDNGYPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEAKPDDSSLPIIGRVAAGAPILAEQHIEESCNINPAFFHPRADYLLRVHGMSMKDIGIFDGDLLAVHTTREARNGQVVVARIGDEVTVKRFKREGSKVWLIAENPEFAPIEVNLKDQDLVIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain 55989 / EAEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O157:H7
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.312 kDa
Sequence
MKVLTARQQQVYDLIRDHIAHSGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVGRVAAGEPLLAQEHIECRYQVDPAMFKPSADFLLRVSGMSMKNIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKKQGNTVHLLAENEEFAPIVVDLRQQSFSIEGLAVGVIRNSDWS

Gene
lexA
Protein
LexA repressor
Organism
Pectobacterium carotovorum subsp. carotovorum
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.317 kDa
Sequence
MKVLTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVGRVAAGEPLLAQEHIECRYQVDPAMFKPSADFLLRVSGMSMKNIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKKQGNTVHLLAENEEFAPIVVDLRQQSFSIEGLAVGVIRNSDWS

Gene
lexA
Protein
LexA repressor
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.329 kDa
Sequence
MKVLTARQQQVYDLIRDHIAQTGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVGRVAAGEPLLAQEHIECHYQVDPAMFKPSADFLLRVSGMSMKDIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKKQGNMVHLLAENEEFAPIVVDLRQQSFSIEGLAVGVIRNSDWS

Gene
lexA
Protein
LexA repressor
Organism
Clostridium kluyveri (strain NBRC 12016)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.201 kDa
Sequence
MTERSNNRQSQIYNFIKSQIKQKGYPPSVREICTAVGLKSTSTVHSYLEKLERRGFIKRDATKSRTIEVIEKSQKKEMIEVPIIGTITAGMPIIAVENIEDYFPLPMDYIKNKREIFMLRVKGESMVDAGILDGDLSLIEKVHSAENGDIVVALIENEATLKRFFKEENHIRLQPENKNMPPIIVDDCKIIGRLIGIYRQYE

Gene
lexA
Protein
LexA repressor
Organism
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
23.201 kDa
Sequence
MTERSNNRQSQIYNFIKSQIKQKGYPPSVREICTAVGLKSTSTVHSYLEKLERRGFIKRDATKSRTIEVIEKSQKKEMIEVPIIGTITAGMPIIAVENIEDYFPLPMDYIKNKREIFMLRVKGESMVDAGILDGDLSLIEKVHSAENGDIVVALIENEATLKRFFKEENHIRLQPENKNMPPIIVDDCKIIGRLIGIYRQYE

Gene
lexA
Protein
LexA repressor
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.367 kDa
Sequence
MKALTTRQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEENGLPLIGRVAAGEPLLAQQHIEGHYQVDPGLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNTVELLPENSEFKPIVVDLREHNFSIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.212 kDa
Sequence
MKLTARQSQVLDIIRRYVDETGYPPTRAEIAAELGFRSANAAEEHLRALARKGAIEMVPGASRGIRLPEAEEDLGLPVIGQVAAGSPILAQEHIEDHCTLQPGFFSPSADYLLRVRGMSMKDIGILDGDLLAVHSTQDVHNGQIVVARVGEEVTVKRFRREGNKVWLIAENEEFAPIEVDLAEQELFIEGLGVGVIRRSDLH

Gene
lexA
Protein
LexA repressor
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.233 kDa
Sequence
MKPLTVRQREILDCIRRSVENEGFPPTIAEIARAIGVSSPHGVREQLRALERKGVIELIPSASRGIRLLARAEEPGLPLIGKVAAGRPLLTEAQVERYCQLGPELFEHKGDYLLRVQGMSMRDAGIIDGDLLVVQQAQEARSGQIVVVRLHDEVTVKRLRLEGALAYLEPANPEFSVIAVDPERQPLCIEGIVVGVIRTRVG

Gene
lexA
Protein
LexA repressor
Organism
Verrucomicrobium spinosum (strain ATCC 43997 / DSM 4136 / JCM 18804 / IFAM 1439)
Length
202 amino acids
Function
Binds the consensus sequence 5'-TGTTC-N(4)-GAACA-3'; some genes have a tandem consensus sequence, at high concentrations their binding is cooperative (PubMed:27489856). Binds to the promoters of a number of genes, including dinB, imuA, lexA, recA, recQ, splB and uvrA (PubMed:27489856). Represses a number of genes involved in the response to DNA damage (SOS response) (By similarity). In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair (By similarity).
Similarity
Belongs to the peptidase S24 family.
Mass
22.718 kDa
Sequence
MLTERQQELLDFLRVYQRQQGVMPSTRDIQLHFGFASQTAAMSHLKALERKGVIRRLAGKARAVVFPEVMERETVDIPIFGLIPAGFTADNPEHSDGNLTLDLRTMGLSPRSKPFALKVRGDSMTGAHIIQGDYVILEQRDPRPKDIVAALMDGETTLKRYLVDNGQPFLRAENPSYPDLIPARELMIQGVMVGLFRPYNGR

Gene
lexA
Protein
LexA repressor
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shigella boydii serotype 4 (strain Sb227)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shigella flexneri serotype 5b (strain 8401)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shigella flexneri
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Shigella sonnei (strain Ss046)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Sodalis glossinidius (strain morsitans)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.23 kDa
Sequence
MKALTTRQKEVFDLIRDHITQTGMPPTRAEIASRLGFRSPNAAEEHLKALARKGAIEIVSGASRGIRLMIEEESGLPLIGRVAAGEPLLATQHIESHYQVDPALFKPHADFLLRVSGMSMKDIGIMDGDLLAVHKTQDACNGQVVVARIDDDVTVKRLKRQGNIVELLPENSEFDPIVVDLRQQELTIEGLAVGVIRNGNWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O81 (strain ED1a)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O8 (strain IAI1)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain K12 / DH10B)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O9:H4 (strain HS)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O1:K1 / APEC
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain K12)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847).The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in response to DNA damaging agents that is mediated by RecA and LexA (PubMed:22412352).
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain SE11)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Escherichia coli (strain UTI89 / UPEC)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.358 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL

Gene
lexA
Protein
LexA repressor
Organism
Edwardsiella ictaluri (strain 93-146)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.428 kDa
Sequence
MKALTARQQQVYDLIRDHIEQTGMPPTRAEIAQRLGFRSPNAAEEHLKALQRKGVIEIVSGASRGIRLLMEDETGLPLVGQVAAGEPLLAQQHIEGFYQIDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIEDEVTVKRLKKQGNMVQLLPENCDFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Enterobacter sp. (strain 638)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.204 kDa
Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVLEIVSGASRGIRLLVEEETGIPLIGRVAAGEPLLAQQHIEGHYQVDPGMFKPSADFLLRVSGMSMKDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNTVQLLPENSEFSPIVVDLREQTFSIEGLAVGVIRNGEWL

Gene
lexA
Protein
LexA repressor
Organism
Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.172 kDa
Sequence
MKALTARQQQVYDLIRDHINQTGMPPTRAEIAAQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLMMEDESGLPLIGRVAAGEPLLAEQHIEGHYQVDPGLFKPGADFLLRVSGMSMKNIGIMDGDLLAVHKTEDVRNGQVVVARIDDEVTVKRLKKNGNMVELLPENPDFQPIVVDLRQQTLTIEGLAVGVIRNGNWL

Gene
lexA
Protein
LexA repressor
Organism
Pseudomonas putida
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.148 kDa
Sequence
MLKLTPRQAEILAFIKRCLEDNGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGLEAKAEEAGLPIIGRVAAGAPILAEQHIEQSCNINPAFFHPQADYLLRVHGMSMKDVGIFDGDLLAVHTCREARNGQIVVARIGDEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELVIEGLSVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.267 kDa
Sequence
MKDLTEKQEFVLQYISDTVREKGFPPTIREIGDQFGITAKGAYDHLKAIEKKGYIRTSKNQSRAIELLKGNADEALLVRASGIPLLGQVAAGAPILAEENIEEYIAVPDDLATKPGTFALRVKGDSMVEAGISDGDIAIIQKKDTARNGEIVVALIENEATLKVFFKEPDMIRLEPRNAKLKPIRTKKATIIGKLIGLYRIY

Gene
lexA
Protein
LexA repressor
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.267 kDa
Sequence
MKDLTEKQEFVLQYISDTVREKGFPPTIREIGDQFGITAKGAYDHLKAIEKKGYIRTSKNQSRAIELLKGNADEALLVRASGIPLLGQVAAGAPILAEENIEEYIAVPDDLATKPGTFALRVKGDSMVEAGISDGDIAIIQKKDTARNGEIVVALIENEATLKVFFKEPDMIRLEPRNAKLKPIRTKKATIIGKLIGLYRIY

Gene
lexA
Protein
LexA repressor
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.39 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEDGLPLIGRVAAGEPLLAQQHIEGHYKVDPSMFKPSADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVQLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pestis
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pestis bv. Antiqua (strain Nepal516)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pestis (strain Pestoides F)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
Length
202 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.365 kDa
Sequence
MKALTTRQQEVYDLVRDHLAQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEEEGLPLIGRVAAGEPLLAQQHIEGHYKVDPSLFKPGADFLLRVNGMSMRDIGILDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNIVHLLPENSEFQPIVVDLREQSFTIEGLAVGVIRNGDWI

Gene
lexA
Protein
LexA repressor
Organism
Clostridium botulinum (strain ATCC 19397 / Type A)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.578 kDa
Sequence
MNKSRIDKQNEVYNFIKLQIKEKGYPPSVREICKAVGLSSTSSVHFHLKRLEKEGLIKRDSSKTRAIEIVDPTSKKEVINVPIVGTITAGNPILAIENIEDVFPLPIDYVKNTKDLFMLKVSGESMIEAGILNGDLAIIEKTDSANNGDIVVALIDNEATLKRFFKESSYIRLQPENKSMKPIILENCKVLGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium botulinum (strain 657 / Type Ba4)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.579 kDa
Sequence
MNKSRIDKQNEVYNFIKLQIKEKGYPPSVREICKAVGLSSTSSVHFHLKRLEKEGLIKRDSSKTRAIEIVDPTSKKEVINVPIVGTITAGNPILAIENIEDVFPLPIDYVKNTKDLFMLKVSGESMIEAGILDGDLAIIEKTDSANNGDIVVALIDNEATLKRFFKESSYIRLQPENKSMKPIILENCKVLGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.578 kDa
Sequence
MNKSRIDKQNEVYNFIKLQIKEKGYPPSVREICKAVGLSSTSSVHFHLKRLEKEGLIKRDSSKTRAIEIVDPTSKKEVINVPIVGTITAGNPILAIENIEDVFPLPIDYVKNTKDLFMLKVSGESMIEAGILNGDLAIIEKTDSANNGDIVVALIDNEATLKRFFKESSYIRLQPENKSMKPIILENCKVLGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.227 kDa
Sequence
MEQLTARQTEVLQIITRHLETCGYPPTLREIAAQLGISGTLGVMKHLEALEKKGYLRRQEGSTRGITLCNQSQAASLPIVGVVRAGLLHPAIQDIEGHFAIDRSQLASGGAFFLRVKGDSMVHAHIVEGDLALVRPQPHASNRDIVVAMVDGEATLKRFYREADRIRLQPENPNYEPIIIEKGEQEVSIVGKVVGIYRQME

Gene
lexA
Protein
LexA repressor
Organism
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.02 kDa
Sequence
MEELTPRQNEVLRFLEGYLTQYGYPPTMRDIAAHLRISGTLGVSKHLTALERKGYIRRDPGNSRGISLVGHGSKSASLPIAGVVRAGMLQPAIEDIEGYLAIDQAQLKGGKFFLRVKGDSMVNAAILDGDLALIRPQPTAENNDIVVAMVDGEATLKAFYRERGQIRLQPRNPNMEPIIIREGEGEVAIVGKVVGIFRTLE

Gene
lexA
Protein
LexA repressor
Organism
Geobacter sp. (strain M21)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.289 kDa
Sequence
MEQLTARQTEVLQIITRHLETCGYPPTLREIAAKLGISGTLGVMKHLEALEKKGYLRRQEGSTRGITLCNQNQATSLPIVGVVRAGLLHPAIQDIEGHFAIDRSQLASGGAFFLRVKGDSMIHAHIVEGDLALVRPQPDASNRDIVVAMVEGEATLKRFYREADRIRLQPENPNYEPIIIQKGEQEVSIVGKVVGIYRQME

Gene
lexA
Protein
LexA repressor
Organism
Geobacter uraniireducens (strain Rf4)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
21.655 kDa
Sequence
MEKLTPRQQMVLAFISAHLESHGYPPTLREIGGHLGINGTLGVMKHLDALERKGFITRNAGSSRGIVLVGAVAATSIPIVGVVRAGALQPAIEDIEGYFAVDRALVKGADCFFLRVKGDSMIEAGIRSGDLALVRPQATADNGDIVVARINDEATLKRFFREKDRIRLQPENSAMEPIIVKAKAGEVNIIGKVTGIFRSLE

Gene
lexA
Protein
LexA repressor
Organism
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.35 kDa
Sequence
MYKLTTRQQEVLDLIKSHIEDTGYPPTRAEIANQLGFRSANAAEEHLKALARKGAIEMVPGASRGIRLPETIQGIPLIGRVAAGNPILAEQNIEDYCDVPPDFFYPQANYLLKVQGMSMRDAGILDGDLLAVHSTTQVKNGDIVVARIEDEVTVKRFKRERNNATIQLLPENPDFNIIEVDLRDANFSIEGLSVGIIRREL

Gene
lexA
Protein
LexA repressor
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.059 kDa
Sequence
MKALTARQQQVYDLVRDHISQTGMPPTRAEIAARLGFRSPNAAEEHLKALARKGVIEIVAGASRGIRLLLEESGLPLIGRVAAGEPLLAQEHIESHYQVDPALFKPSADFLLRVSGMSMKDVGIMDGDLLAVHKTQNVRNGQIIVARIEDEVTVKRFKQTGNKVELLAENPEFKPIEVDLREQGLTIEGLAVGVIRNGNWS

Gene
lexA
Protein
LexA repressor
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.059 kDa
Sequence
MKALTARQQQVYDLVRDHISQTGMPPTRAEIAARLGFRSPNAAEEHLKALARKGVIEIVAGASRGIRLLLEESGLPLIGRVAAGEPLLAQEHIESHYQVDPALFKPSADFLLRVSGMSMKDVGIMDGDLLAVHKTQNVRNGQIIVARIEDEVTVKRFKQTGNKVELLAENPEFKPIEVDLREQGLTIEGLAVGVIRNGNWS

Gene
lexA
Protein
LexA repressor
Organism
Dechloromonas aromatica (strain RCB)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
21.433 kDa
Sequence
MKLTPRQQEILDFIKSTLEVLGAPPTRMEISSAFGFASPNAAEDHLKALAKKGAIVLEPGSARGIRLVEQLGLPLIGSVAAGSPILAVENMQGRYALDASLFAPKADFLLKVRGLSMIDVGIFDGDLLAVHKTNQARDGQIVVARLDEEVTVKRLERSGGQIRLIAENPDFEPIIVDPEAVDFAIEGIAVGLIRGAVSKLS

Gene
lexA
Protein
LexA repressor
Organism
Clostridium botulinum (strain Kyoto / Type A2)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.579 kDa
Sequence
MNKSRIDKQNEVYNFIKLQIKEKGYPPSVREICKAVGLSSTSSVHFHLKRLEKEGLIKRDSSKTRAIEIVDPTSKKEVINVPIVGTITAGNPILAIENIEDVFPLPIDYVKNTKDLFMLKVSGESMIEAGILDGDLAIIEKTDSANNGDIVVALIDNEATLKRFFKESSYIRLQPENKSMKPIILENCKVLGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium botulinum (strain Okra / Type B1)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.579 kDa
Sequence
MNKSRIDKQNEVYNFIKLQIKEKGYPPSVREICKAVGLSSTSSVHFHLKRLEKEGLIKRDSSKTRAIEIVDPTSKKEVINVPIVGTITAGNPILAIENIEDVFPLPIDYVKNTKDLFMLKVSGESMIEAGILDGDLAIIEKTDSANNGDIVVALIDNEATLKRFFKESSYIRLQPENKSMKPIILENCKVLGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.579 kDa
Sequence
MNKSRIDKQNEVYNFIKLQIKEKGYPPSVREICKAVGLSSTSSVHFHLKRLEKEGLIKRDSSKTRAIEIVDPTSKKEVINVPIVGTITAGNPILAIENIEDVFPLPIDYVKNTKDLFMLKVSGESMIEAGILDGDLAIIEKTDSANNGDIVVALIDNEATLKRFFKESSYIRLQPENKSMKPIILENCKVLGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Clostridium botulinum (strain Loch Maree / Type A3)
Length
201 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.579 kDa
Sequence
MNKSRIDKQNEVYNFIKLQIKEKGYPPSVREICKAVGLSSTSSVHFHLKRLEKEGLIKRDSSKTRAIEIVDPTSKKEVINVPIVGTITAGNPILAIENIEDVFPLPIDYVKNTKDLFMLKVSGESMIEAGILDGDLAIIEKTDSANNGDIVVALIDNEATLKRFFKESSYIRLQPENKSMKPIILENCKVLGRLVGIYRKY

Gene
lexA
Protein
LexA repressor
Organism
Cellvibrio japonicus (strain Ueda107)
Length
200 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.342 kDa
Sequence
MYNLTSRQEQVLQLIKQYTEETGYPPTRAEIARILGFKSANAAEEHIKALARKGAIEIMPGASRGIRLTESQSGIPIVGRVAAGNPILAQEHIEDYCNIPNSFFSPSADYFLRVHGMSMKDAGILDGDLLAVHRTDQVRNGQIVVARIGEEVTVKRFKRQGNQAQVELWPENPDFKVIHVDMRDQEFSIEGLSVGVIRRD

Gene
lexA
Protein
LexA repressor
Organism
Hahella chejuensis (strain KCTC 2396)
Length
200 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.248 kDa
Sequence
MIKLTKRQEQVLQLIREHIEETGYPPTRAEISNRLGFRSANAAEEHLKALAKKGAIEMVPGASRGIRLPASETQNQGIPIVGQVAAGYPILAQENIEEYCELPPSFFTPSADYFLRVKGMSMKDVGILDGDLLAVHRTTDIHNGQIVVARIGDEVTVKRFQRQKNKVLLLPENEEFEPIEVNLSQQPLDIEGLGVGVIRR

Gene
lexA
Protein
LexA repressor
Organism
Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1)
Length
200 amino acids
Function
Binds a consensus sequence 5'-TGTTC-N(4)-GAACA-3'; some genes have a tandem consensus sequence and their binding is cooperative (PubMed:27489856). Binds to the promoters of a number of genes, including lexA and splB (PubMed:27489856). Represses a number of genes involved in the response to DNA damage (SOS response).
Similarity
Belongs to the peptidase S24 family.
Mass
22.421 kDa
Sequence
MLTEKQEAILDYIRSVQAQRGVPPSTREIQRHFGYESQNAAMNHLRALARKGQLHQVDGATWGLKVSEVQGHFELPIYGTIPAGVPSMQEQQPKETITFDPAVFRLRRPERLWGLEVHGDSMIDAHILDGDIAVLERREAKPGDIVAALVDETTTTLKRLAYVKGKPVLKPENARYALIVPKDRLEIQGVFVGLIGRAKR

Gene
lexA
Protein
LexA repressor
Organism
Clostridium tetani (strain Massachusetts / E88)
Length
200 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.731 kDa
Sequence
MARQNKQEAIYEFIKEQLREKGYPPSVREICNAVELRSTSTVHGHLKRLEEKGVIRRDPTKPRAIEVLEHSIMKKEMVDIPVVGTVTAGKPILAVENIEDTFALPINYVRNKKQLFALKIKGDSMIDTGILDGDLAIVEKNNSVLNGEIVVALLGDRATVKRFFKEKDYIRLQPENETMEPIIVKQCEIIGKVVGVYRKY

Gene
lexA
Protein
LexA repressor
Organism
Teredinibacter turnerae (strain ATCC 39867 / T7901)
Length
200 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.164 kDa
Sequence
MIKLTARQQQILDLIRDHIAETGYPPTRAEIAEILGFKSANAAEEHLKALARKGAIEMIAGASRGIRLPEVQSGIPLVGRVAAGSPILAQEHIEDYCDIPHNFFSPKADFLLTVHGMSMKDIGILDGDLLAVHKTDQVRNGDIVVARIDNEVTVKRFKRERNRAQVELWPENPDFNVIEVDLRDANFAIEGLSVGVIRRS

Gene
lexA
Protein
LexA repressor
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Length
200 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
21.604 kDa
Sequence
MRDLTPRQEEILNLIREWIDTTGSPPTRAEIAQHFGFSSPNAAEQHLKTLAKKGALELVSGASRGIRLPGGGGLAVVGQVAAGSPILAQENIERHVQVDTALFSPRADYLLKVRGQSMKDIGILDGDLLAVHRSAEARAGQVVVARIGDEVTVKRFQKRGHTVQLLPENADFEPIVVDLKRQELVIEGIAVGVIRSGRSL

Gene
lexA
Protein
LexA repressor
Organism
Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO)
Length
200 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.519 kDa
Sequence
MKKELTDRQKKILDFVLSYIDSHGYPPSIRDIARAFRITPRGAIVHLNALEKKGYLTRGKRARSIKVLNRSEAIRLPVVGTIAAGNAIEAIENPTEIIEVPKAMIKIGFDHFLLRVRGESMIEEHILDKDYVVIRKQNTANNGDIVAVLTNSNEATLKKIYIEPEKIILKPANSKMQPIELKPENVKILGKMVGVIRIYG

Gene
lexA
Protein
LexA repressor
Organism
Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429)
Length
199 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.772 kDa
Sequence
MKKLTEKQQKVLDFIKNYIQQNGYSPSIRDIAKHFKLTPRGAHIHVIALEKKGYITRNPKNSRSISLVKRQESILIPVKGKISAGMGIEMFEIVDEEIEIPVRMISGFGNYFALKVEGNSMIDAHIINGDYVILKKQYRIPNGQIAAVVFDNKVTLKRFYHKKDKVELVPENKDMNPIVCDAKDIKVIGKLVGIIRFYE

Gene
lexA
Protein
LexA repressor
Organism
Thermosipho africanus (strain TCF52B)
Length
198 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.46 kDa
Sequence
MKELTNRQKMVLDFITSYIQQNGYSPSIRDIAKHFKLTPRGAHIHVLALEKKGYITRNPKNSRSISLVKRPETVSIPVKGKISAGQGIEMFELVDEEIEIPVRMINGYGNYFALRVEGTSMIEAHIIDGDYVILKKQYRIPNGQIAAVVFDNKVTLKRFYHKNDKVELVPENSSMSPIICDAKDVKVIGKLVGVIRIY

Gene
lexA
Protein
LexA repressor
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Length
197 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.864 kDa
Sequence
MKDLTERQRKVLLFIEEFIEKNGYPPSVREIARRFRITPRGALLHLIALEKKGYIERKNGKPRALRISKSIRNKIPLIGEIRAGEKREAIEYLEDYIEIPESFLSSGYDHFLLKVKGESMIEEHICDGDLVLVRRQDWAQNGDIVAAMVDGEVTLKKFYQRGDTVELRPANREMSSMFFRAEKVKILGKVVGVFRKL

Gene
lexA
Protein
LexA repressor
Organism
Thermotoga neapolitana
Length
197 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.708 kDa
Sequence
MKDLTAKQRSVLIFIEEFIEKNGYPPSVREIARRFRITPRGAQLHLVALEKKGYIERKNGKPRAMRVTKSVKNRVPLIGEIRAGEKKEAIEYLEDYIEVPGSFLSSGYEHFLLRVKGESMIEEHICDGDLVLIRRQDWAQNGDIVAAMVEGEVTLKKFFQRGEMVELRPANKEMSPMFFRADRVKILGKVVGVFRKI

Gene
lexA
Protein
LexA repressor
Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Length
197 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.836 kDa
Sequence
MKDLTERQRKVLLFIEEFIEKNGYPPSVREIARRFRITPRGALLHLIALEKKGYIERKNGKPRALRVSKSIRNKIPLIGEIRAGEKREAVEYLEDYIEIPESFLSSGYDHFLLKVKGESMIEEHICDGDLVLVRRQDWAQNGDIVVAMVDGEVTLKKFYQRGDTVELRPANREMSSMFFKAEKVKILGKVVGVFRKL

Gene
lexA
Protein
LexA repressor
Organism
Thermotoga sp. (strain RQ2)
Length
197 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
22.822 kDa
Sequence
MKDLTERQRKVLLFIEEFIEKNGYPPSVREIARRFRITPRGALLHLIALEKKGYIERKNGKPRALRVSKSIRNKIPLIGEIRAGEKREAIEYLEDYIEIPESFLSSGYDHFLLKVKGESMIEEHICDGDLVLVRRQDWAQNGDIVAAMVDGEVTLKKFYQRGDTVELRPANREMSSMFFKAEKVKILGKVVGVFRKL

Gene
lexA
Protein
LexA repressor
Organism
Photobacterium profundum (strain SS9)
Length
192 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
21.099 kDa
Sequence
MIKAKIEDSGMPPTRAEIARELGFRSANAAEEHLKALARKEVIEIVPGASRGIRVLRHDEVEAKGLPLIGRVAAGEPILAQEHVETHYEVDPALFKPRADFLLRVNGMSMKDIGIMDGDLLAVHKTQDVHNGQVVVARVDDDVTVKRLDKQGSQVLLHAENEDFAPIVVDLTHQQLTIEGIAVGVIRTADWM

Gene
lexA
Protein
LexA repressor
Organism
Photobacterium profundum (strain SS9)
Length
192 amino acids
Function
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Similarity
Belongs to the peptidase S24 family.
Mass
21.099 kDa
Sequence
MIKAKIEDSGMPPTRAEIARELGFRSANAAEEHLKALARKEVIEIVPGASRGIRVLRHDEVEAKGLPLIGRVAAGEPILAQEHVETHYEVDPALFKPRADFLLRVNGMSMKDIGIMDGDLLAVHKTQDVHNGQVVVARVDDDVTVKRLDKQGSQVLLHAENEDFAPIVVDLTHQQLTIEGIAVGVIRTADWM