D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase catalyzes the peptide bond cleavage between D-alanyl-D-alanine residues in peptide substrates, member of the peptidase S13 family
D-Ala-D-Ala carboxypeptidase 3 (S13) family; This family of serine peptidases belong to MEROPS ...
35-482
6.92e-124
D-Ala-D-Ala carboxypeptidase 3 (S13) family; This family of serine peptidases belong to MEROPS peptidase family S13 (D-Ala-D-Ala carboxypeptidase C, clan SE). The active site residues occur in the motif SXXK. D-Ala-D-Ala carboxypeptidase C is involved in the metabolism of cell components. There are three families of serine-type D-Ala-D-Ala peptidase (designated S11, S12 and S13), which are also known as low molecular weight penicillin-binding proteins. Family S13 comprises D-Ala-D-Ala peptidases that have sufficient sequence similarity around their active sites to assume a distant evolutionary relationship to other clan members; members of the S13 family also bind penicillin and have D-amino-peptidase activity.
Pssm-ID: 396611 Cd Length: 444 Bit Score: 368.72 E-value: 6.92e-124
D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family; In E. coli, this protein is ...
59-461
3.81e-86
D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family; In E. coli, this protein is known as penicillin binding protein 4 (dacB). A signal sequence is cleaved from a precursor form. The protein is described as periplasmic in E. coli (Gram-negative) and extracellular in Actinomadura R39 (Gram-positive). Unlike some other proteins with similar activity, it does not form transpeptidation. It is not essential for viability. This family is related to class A beta-lactamases. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 200042 [Multi-domain] Cd Length: 333 Bit Score: 267.82 E-value: 3.81e-86
D-Ala-D-Ala carboxypeptidase 3 (S13) family; This family of serine peptidases belong to MEROPS ...
35-482
6.92e-124
D-Ala-D-Ala carboxypeptidase 3 (S13) family; This family of serine peptidases belong to MEROPS peptidase family S13 (D-Ala-D-Ala carboxypeptidase C, clan SE). The active site residues occur in the motif SXXK. D-Ala-D-Ala carboxypeptidase C is involved in the metabolism of cell components. There are three families of serine-type D-Ala-D-Ala peptidase (designated S11, S12 and S13), which are also known as low molecular weight penicillin-binding proteins. Family S13 comprises D-Ala-D-Ala peptidases that have sufficient sequence similarity around their active sites to assume a distant evolutionary relationship to other clan members; members of the S13 family also bind penicillin and have D-amino-peptidase activity.
Pssm-ID: 396611 Cd Length: 444 Bit Score: 368.72 E-value: 6.92e-124
D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family; In E. coli, this protein is ...
59-461
3.81e-86
D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family; In E. coli, this protein is known as penicillin binding protein 4 (dacB). A signal sequence is cleaved from a precursor form. The protein is described as periplasmic in E. coli (Gram-negative) and extracellular in Actinomadura R39 (Gram-positive). Unlike some other proteins with similar activity, it does not form transpeptidation. It is not essential for viability. This family is related to class A beta-lactamases. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 200042 [Multi-domain] Cd Length: 333 Bit Score: 267.82 E-value: 3.81e-86
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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