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mepM

Gene
mepM
Protein
Murein DD-endopeptidase MepM
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
440 amino acids
Function
A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH (By similarity).
Similarity
Belongs to the peptidase M23B family.
Mass
49.058 kDa
Sequence
MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD

Gene
mepM
Protein
Murein DD-endopeptidase MepM
Organism
Escherichia coli (strain K12)
Length
440 amino acids
Function
A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant.
Similarity
Belongs to the peptidase M23B family.
Mass
49.058 kDa
Sequence
MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD

Gene
mepM
Protein
Murein DD-endopeptidase MepM
Organism
Shigella flexneri
Length
440 amino acids
Function
A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH (By similarity).
Similarity
Belongs to the peptidase M23B family.
Mass
49.058 kDa
Sequence
MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD

Gene
mepM
Protein
Murein DD-endopeptidase MepM
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
440 amino acids
Function
A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH (By similarity).
Similarity
Belongs to the peptidase M23B family.
Mass
49.058 kDa
Sequence
MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD

Gene
mepM
Protein
Murein DD-endopeptidase MepM
Organism
Escherichia coli (strain K12)
Length
440 amino acids
Function
A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant.
Similarity
Belongs to the peptidase M23B family.
Mass
49.058 kDa
Sequence
MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD

Gene
mepM
Protein
Murein DD-endopeptidase MepM
Organism
Shigella flexneri
Length
440 amino acids
Function
A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH (By similarity).
Similarity
Belongs to the peptidase M23B family.
Mass
49.058 kDa
Sequence
MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD