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CLPB2

Gene
CLPB2
Protein
Chaperone protein ClpB2, chloroplastic
Organism
Oryza sativa subsp. japonica
Length
978 amino acids
Function
Molecular chaperone that may play a role in chloroplast development.
Similarity
Belongs to the ClpA/ClpB family.
Mass
108.985 kDa
Sequence
MAAAPPLAAGLRPAMAAAQAPVVAAAWGVGARRGAALSSSARCRALRLSRGGGGGRDGWVPPPVVGRMPPRTLSVRCAASNGRITQQEFTEMAWQSIVSSPEVAKESKHQIVETEHLMKSLLEQRNGLARRIFSKAGVDNTRLLDATEKFIQRQPKVLGEDPGSMLGRDLEALIQRARDFKKEYGDSFVSVEHLVLGFAEDKRFGRQLFKDFQITVQSLKTAIESIRGKQNVIDQDPEGKYEALDKYGKDLTAMARQGKLDPVIGRDDEIRRCIQILSRRTKNNPVLIGEPGVGKTAIAEGLAQRIVQGDVPQALTNRRLIALDMGALIAGAKYRGEFEDRLKAVLKEVTDSDGQTILFIDEIHTVVGAGATNGAMDAGNLLKPMLGRGELRCIGATTLDEYRKYIEKDPALERRFQQVYVDQPSVEDTISILRGLRERYELHHGVRISDSALVAAALLSDRYISGRFLPDKAIDLVDESAAKLKMEITSKPTALDEIDRAVIKLEMERLSLTNDTDKASRDRLSRIEAELSLLKEKQKDLTEQWEREKSVMTKIQSIKEEIDRVNVEIQQAEREYDLNRAAELKYGSLNALQRQLQTTEKELDEYQSSGKSMLREEVTQDDIAEIVSRWTGIPVSKLKQSDREKLLYLEEELHKRVVGQDPAVKAVSEAIQRSRAGLSDPNRPIASFMFMGPTGVGKTELAKALAAFMFNTEEAVVRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSIILFDEIEKAHGDVFNVFLQILDDGRVTDSQGRKVSFTNSIIIMTSNVGSQFILNMDEEGGSTDSAYENIKKRVMDAARSVFRPEFMNRIDEYIVFKPLEREQINSIVKLQLARVQKRIADRKIKLEVSPGAVEFLGSLGYDPNYGARPVKRVIQQYVENELAKGILRGDFKDEDSILVDTQVTVPSNGQLPQQKLVFHKMSEESAPAAAEDEKFLPAV

Gene
clpB2
Protein
Chaperone protein ClpB 2
Organism
Synechococcus sp. (strain WH8102)
Length
900 amino acids
Function
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Similarity
Belongs to the ClpA/ClpB family.
Mass
99.782 kDa
Sequence
MTGTPASRGSLTHEPDRFSDPAWELLLAGQDMARRWRHDQLDVEHLIQVLFSDSSFRRWVEPLPLRSDDLLDRLEDVLADQPPARGDQLFIGEDLEQLLETADQVRGRWGDRSIDVPQLIVAVGADPRIGAELFAAQGLAVDRLESLLRQPSVSPAPAPPPVPTAASAPAPTPRSAPAPRVMAPEPEPMVELEREPSALEAYGRDLTEEAEAGSLDPVIGRDSEIRNLIKVLSRRSKNNPVLIGEPGVGKTAIAELLAQRIVAGEVPDSLQGLRLIALDLGALIAGAKFRGQFEERLRSVLEEVSRSDSGVVLFIDELHTVVGSDRSSTDAGSLLKPALARGDLRCIGATTPEEYRRTVEKDPALNRRFQQVLIREPDLELSLEILRGLRERYELHHGVTITDEAIQTANRLADRYISDRCLPDKAIDLIDEAAAQLKIEVTSKPQVVEEAEADLRRVELALLAAEEAPEEERIQLQRQRLEVSSRLDDLRRRWQEERTQLEELGQLLQQDEDLRHAIAEAEREGALEEAARLQYDQLHTVQQRREALEASQAEAQSAGTALLREQVEAGDIADLVARWTGIPVQRLLAGERRKLLALESHLSERVIGQVEAVAAVAAAIRRARAGMKDPRRPVGSFLFLGPTGVGKTELAKALATSLFDEEEALVRLDMSEFMERNASARLIGAPPGYVGYEEGGQLTEAVRRRPYAVLLLDEVEKAHPDVFNLLLQVLDDGRLTDSQGLTVDFRHTVVVMTSNLASPVILEHARSGSSDDAQLQQQVDAALSSQFRPEFLNRIDEVIRFRPLKVKDLVRIVRLQLADLSTLMAEQGLSLEVDDAVADSLARQGHEPEYGARPLRRVLRRQLENPLATQLLEERFRSAHGIRVRCGTDDGASLEFEPLE

Gene
clpB2
Protein
Chaperone protein ClpB 2
Organism
Synechococcus elongatus (strain PCC 7942)
Length
895 amino acids
Function
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Similarity
Belongs to the ClpA/ClpB family.
Mass
99.821 kDa
Sequence
MQPTDPNRFTDQAWDAIVESQTVARQLRQQQLEVEHVLLALLDQESGVAAEILAKAGVAVANLRQPLEDFARRQPRNASGTQLYLGRGLDRLLDLAERARELWQDEFIGVEHLLMGFVEDDRIGRRLAQGLKLDAKTLETTIQALRSPAADEAEAEESEPSYPFLSKYGRDLTALAEQEKLDPVIGRDLEIRRVIQVLSRRSKNNPVLIGEPGVGKTAIAEGLAQRIVAGEVPDSLKQRRLISLDMGSLIAGAKYRGEFEERLRAVLHEVTHSDGQMVLFIDELHTVVGAGAGQQGSAMDAGNLLKPMLARGELRCIGATTTDEYRRTIEKDPALERRFQQVYVSQPSVEDTIAILRGLKERYEGHHGVKITDGALMAAAKLSHRYISDRFLPDKAIDLIDEASAQLKMEITSKPSELEDLERRLLQLEMEQLSLSGENGQASVHSDRLQQIQTELQTLQEQQARLNQQWQQEKQLLEELGRLQEEEETLRQQVNQAEREHDLNKGAELKFGQLEALQQQRQAIEEQIQALHANGQTLLREQVEEADIAEIVARWTNIPVQRLLESERQKLLQLESFLHQRVIGQDEAVVAVAAAIRRARAGMKDPSRPIGSFLFLGPTGVGKTELARALANCLFDAEDALIRFDMSEYMEKNSISRLIGAPPGYIGYEEGGQLSEAIRRHPYAVVLFDEVEKAHPDVFNLLLQVLDDGRITDSQGRTIDFCNAVIVMTSNIGSQFILEMGEEEASLDAVELKVLGALRQHFRPEFLNRIDDTILFQPLSRGQLQQIVDIQLQRLKRLLAEQAIALNVTPAAAANLADRGYDPVYGARPLKRAIQRLIENPVASLILEQQFDAGDALIVDVDAEGQLQFQVSKPVTATVVEPDDSPAIAVEAIPS

Gene
clpB2
Protein
Chaperone protein ClpB 2
Organism
Thermosynechococcus elongatus (strain BP-1)
Length
887 amino acids
Function
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Similarity
Belongs to the ClpA/ClpB family.
Mass
99.84 kDa
Sequence
MQPTDPTKFTDKAWEAIVKSQDVAREYRSQYLETEHVMIALLREEGLGQVILERSDIDTEWVLKRLMDFARQQPRVPAGSELYCGRSLDALLDEANRLRQEEEDQFISIEHLLLAFVGDRRIGQRLFRALNCDRQQLAATVKAIRGAQKVLDQNPENKYAALEKYGRDLTEAARQGKLDPVIGRDEEIRRVIQVLSRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGDVPESLKNRRLISLDLGSLVAGAKFRGDFEDRLKAVLHEVTHSEGQIVLFIDELHTVVGAGANQNSSMDASNLLKPMLARGELRCIGATTLDEYRKYIEKDAALERRFQQVYIGQPSVEDTISILRGLKDRYEIHHNVKITDSALVAAAMLSDRYISDRYLPDKAIDLVDEAAAKLKMEITTKPAELEALERRLRQLEMERLSLKQEESLPLSQAPLQATRDRLQRIEAEIAQLQPRQQAMQARWQAEKELLERINSLKEEEDQVKLQIEQAERDYNLNKAAQLKYGRLETLQRELEATEAQLLELQAAGGTFLRDQVTEADIAEIVAKWTGIPLQKLMASERQKLLQLEQVLHQRVIGQSDAVAAVAAAIRRARAGMKDPARPIGSFLFMGPTGVGKTELARALAEALFDDENALVRIDMSEYMEKHAVSRMIGAPPGYVGFDSGGQLTEAIRRRPYAVVLFDEVEKAHPEVFNVLLQVLDDGRITDSQGRTVDFRNTVIIMTSNLGSEHILDLAADDSRYEEMRQRVLQSAQKYFRPEFLNRIDDVILFHGLGRTELAQIAQIQLRRVEKLLADQKIHLRLTPAALDHLVAVGFDPVYGARPLKRAIQRELENPLAVKLLEEVFTPGDTILVDLVGSELTFRAVSPAGTGDRDTVSAS

Gene
clpB2
Protein
Chaperone protein ClpB 2
Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Length
879 amino acids
Function
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Similarity
Belongs to the ClpA/ClpB family.
Mass
98.274 kDa
Sequence
MDMNRLTQKSQEALQEAQTAAGRMGHTEVDGEHLLLALLDQEDGLIPRLLQQAGTEPKELRAAVREELSHRPKATGPGAAPGQVFVTQRLARLLDAAEREAKRLKDEYVSVEHLLLALAEESSSTAAGLLLKQAGITRDSFLSALTQVRGNQRVTSANPEVAYEALEKYGRDLVLEARSGRLDPVIGRDAEIRRVTQILSRKTKNNPVLIGDPGVGKTAIVEGLAQRIVRGDVPEGLRDKTVFALDMGSLVAGAKYRGEFEERLKAVLSEVKAAEGRILLFVDELHTVVGAGAAEGAMDAGNMLKPMLARGELHMIGATTLDEYRKHIEKDAALERRFQQVLVDEPSVEDTISILRGLRERLEVFHGVKIQDTALVSAATLSHRYITDRFLPDKAIDLVDEACARLRTEIDSMPAELDEITRRVTRLEIEEAALSKESDPASKTRLEELRRELADLRGEADAKHAQWEAERQAIRRVQELRQELEQVRHEAEEAERAYDLNRAAELRYGRLQDLERRLAAEEEQLAAKQGENRLLREVVTEEEIAEIVAAWTGIPVARLQEGEREKLLRLDEILRERVIGQDEAVKLVTDAIIRARSGIRDPRRPIGSFIFLGPTGVGKTELAKTLARTLFDSEENMVRLDMSEYQERHTVSRLMGAPPGYVGYEEGGQLTEAVRRKPYSVVLFDEIEKAHTDVFNTLLQILDDGRITDAQGRTVDFRNTVIIMTSNIGSEHLLDGATAEGEIKPDARALVMGELRGHFRPEFLNRVDDIVLFKPLGERQIERIVELQFDELRQRLAERRITVELTDAGREVIAHQGYDPVYGARPLRRYISHEVETLVGRALLRGDVQDGATVRVDAEHGELVVTYDQPEDVKGAWAA

Gene
clpB2
Protein
Chaperone protein ClpB 2
Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Length
872 amino acids
Function
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Similarity
Belongs to the ClpA/ClpB family.
Mass
98.624 kDa
Sequence
MQPTNPNQFTEKAWEAIAHTPEIAKQHQQQQIESEHLMKALLEQDGLASGILTKAGVNLQKISDRTEQYIQRQPKVSGNSTSVYLGRSLDTLLDRAEAHRKDFQDEYISIEHLLLAYPKDDRFGKGLFQEFALDESKLKNIIKQVRGSQTVTDQNPEGKYQSLEKYGRDLTEAARKGQLDPVIGRDDEIRRTIQILSRRTKNNPVLIGEPGVGKTAIAEGLAQRIVAGDVPQSLKDRKLISLDMGAMIAGAKFRGEFEERLKAVLKEVTESGGNIVLFIDEIHTVVGAGATQGAMDAGNLLKPMLARGELRCIGATTLDEYRKYIEKDAALERRFQQVYVDQPSVEDTISILRGLKERYEVHHGVKISDSSLVAAATLSSRYISDRFLPDKAIDLVDEAAARLKMEITSKPEELDEIDRKILQLEMEKLSLQKESDAASRERLERLEKELADLKEEQRTLNTQWQSEKDVINKLQSVKEEIDKVNLEIQQAERNYDLNRAAELKYGNLTDLHRRLEATERELSQTQGTGKSLLREEVTEADIAEIISKWTGIPISKLVESEKEKLLHLEDELHHRVIGQDEAVTAVADAIQRSRAGLADPNRPTASFVFLGPTGVGKTELAKALASYMFDTEDALVRIDMSEYMEKHAVSRLIGAPPGYVGYEEGGQLTETIRRRPYAVILFDEIEKAHPDVFNIFLQILDDGRVTDAQGHTVDFKNTIIIMTSNIGSQYILDIAGDNSRYDEMRHRVMEAMRNSFRPEFLNRIDEVIIFHSLDKKELRQIVQLQVERLKARLDDRKISLRLSDVALDFLAEVGYDPVFGARPLKRAIQRELETQIAKAILRGEFNDGDTIFVDVQNERLSFSRLPVEVFSS

Gene
clpB2
Protein
Chaperone protein ClpB 2
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
872 amino acids
Function
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Similarity
Belongs to the ClpA/ClpB family.
Mass
98.123 kDa
Sequence
MQPTDPNKFTEKAWEAIAKTPEIAKQHRQQQIETEHLLSALLEQNGLATSIFNKAGASIPRVNDQVNSFIAQQPKLSNPSESIYLGRSLDKLLDNAEIAKSKYGDDYISIEHLMAAYGQDDRLGKNLYREIGLTENKLAEIIKQIRGTQKVTDQNPEGKYESLEKYGRDLTELAREGKLDPVIGRDEEVRRTIQILSRRTKNNPVLIGEPGVGKTAIAEGLAQRIINHDVPESLRDRKLISLDMGALIAGAKYRGEFEERLKAVLKEVTDSQGQIILFIDEIHTVVGAGATQGAMDAGNLLKPMLARGALRCIGATTLDEYRKYIEKDAALERRFQEVLVDEPNVLDTISILRGLKERYEVHHGVKIADSALVAAAMLSNRYISDRFLPDKAIDLVDEAAAKLKMEITSKPEELDEVDRKILQLEMERLSLQRENDSASKERLEKLEKELADFKEEQSKLNGQWQSEKTVIDQIRTVKETIDQVNLEIQQAQRDYDYNKAAELQYGKLTDLQRQVEALETQLAEQQTSGKSLLREEVLESDIAEIISKWTGIPISKLVESEKEKLLHLEDELHSRVIGQDEAVTAVAEAIQRSRAGLSDPNRPTASFIFLGPTGVGKTELAKALAKNLFDTEEALVRIDMSEYMEKHAVSRLMGAPPGYVGYEEGGQLTEAIRRRPYSVILFDEIEKAHGDVFNVMLQILDDGRLTDAQGHVVDFKNTIIIMTSNLGSQYILDVAGDDSRYEEMRSRVMDVMRENFRPEFLNRVDETIIFHGLQKSELRSIVQIQIQSLATRLEEQKLTLKLTDKALDFLAAVGYDPVYGARPLKRAVQKYLETAIAKGILRGDYKPGETIVVDETDERLSFTSLRGDLVIV

Gene
CLPB2
Protein
Putative chaperone protein ClpB2, chloroplastic
Organism
Arabidopsis thaliana
Length
623 amino acids
Similarity
Belongs to the ClpA/ClpB family.
Mass
68.898 kDa
Sequence
MNDLKFDPNVKLILASARSHAMSLSHGQVTPLHLGVTLISDLTSVFYRAITSAGDGDISAQSVVNVINQSLYKLTKRNLGDTKVGVAVLVISLLEDSQISDVLKEAGVVPEKVKSEVEKLRGEVILRALKTYGTDLVEQAGKLDPVIGRHREIRRVIEVLSRRTKNNPVLIGEPGVGKTAVVEGLAQRILKGDVPINLTGVKLISLEFGAMVAGTTLRGQFEERLKSVLKAVEEAQGKVVLFIDEIHMALGACKASGSTDAAKLLKPMLARGQLRFIGATTLEEYRTHVEKDAAFERRFQQVFVAEPSVPDTISILRGLKEKYEGHHGVRIQDRALVLSAQLSERYITGRRLPDKAIDLVDESCAHVKAQLDIQPEEIDSLERKVMQLEIEIHALEKEKDDKASEARLSEVRKELDDLRDKLEPLTIKYKKEKKIINETRRLKQNRDDLMIALQEAERQHDVPKAAVLKYGAIQEVESAIAKLEKSAKDNVMLTETVGPENIAEVVSRWTGIPVTRLDQNEKKRLISLADKLHERVVGQDEAVKAVAAAILRSRVGLGRPQQPSGSFLFLGPTGVGKTELAKALAEQLFDSENLLVRLDMSEYNDKFSVNKLIGAPPGYVHWS

Gene
clpB2
Protein
Probable chaperone protein ClpB 2
Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Length
442 amino acids
Function
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Similarity
Belongs to the ClpA/ClpB family.
Mass
48.929 kDa
Sequence
MHFDPNKFTVKAQEALQAASMLASSKQNQQIEPEHLLSVMLGDHDNIACQIARKLETPVDTLLSVVDREIDRIPKVTGASATGQYISSDLGKVFDTALKEAEQLKDEYISSEHLFIAMSEAGVKVSKLLKDAGIDRNAILKVLTSFRGSQRVTSQNAEESYQSLKKYSRNLNDLVIKGKLDPVIGRDDEIRRVLQILSRRTKNNPVLIGEPGVGKTAIVEGIAQRIVGGDVPENLKSKQIAALDIAALVAGTKFRGEFEERLKALVKEVQASDGEVILFIDELHLLVGAGSAEGSMDAANILKPALARGELRCIGATTLDEYRKHIEKDAALERRFQTVIVDQPSVEDTVSILRGLKEKYEIHHGVRIKDAALVAAAELSNRYIADRFLPDKAIDLIDEACSRLRLEIDSEPEELDRINRELRRLEIEREALKRELEATGSV