metalloprotease PmbA is involved in CcdA degradation, suppressing the inhibitory activity of the carbon storage regulator (CsrA), proteolytic processing of the antibiotic microcin B17, and in sensitivity to the DNA gyrase inhibitor LetD
PmbA/TldA metallopeptidase C-terminal domain; This entry represents a group of ...
241-449
1.33e-91
PmbA/TldA metallopeptidase C-terminal domain; This entry represents a group of metalloproteases. The tertiary structure of the Escherichia coli TdlD/TdlE complex has been solved, and shows that the TdlD subunit is the active peptidase, binding a single zinc ion at an HEXXXH motif in which the glutamic acid is a substrate-binding residue and the two histidines are zinc ligands. The third zinc ligand is a cysteine, C-terminal to the HEXXXH motif. The TldE (also known as PmbA) by itself has no catalytic activity, does not bind zinc, and does not carry the HEXXXH motif. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation.
Pssm-ID: 437121 Cd Length: 221 Bit Score: 276.69 E-value: 1.33e-91
PmbA/TldA metallopeptidase C-terminal domain; This entry represents a group of ...
241-449
1.33e-91
PmbA/TldA metallopeptidase C-terminal domain; This entry represents a group of metalloproteases. The tertiary structure of the Escherichia coli TdlD/TdlE complex has been solved, and shows that the TdlD subunit is the active peptidase, binding a single zinc ion at an HEXXXH motif in which the glutamic acid is a substrate-binding residue and the two histidines are zinc ligands. The third zinc ligand is a cysteine, C-terminal to the HEXXXH motif. The TldE (also known as PmbA) by itself has no catalytic activity, does not bind zinc, and does not carry the HEXXXH motif. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation.
Pssm-ID: 437121 Cd Length: 221 Bit Score: 276.69 E-value: 1.33e-91
PmbA/TldA metallopeptidase central domain; This entry represents a group of metalloproteases. ...
127-234
4.59e-15
PmbA/TldA metallopeptidase central domain; This entry represents a group of metalloproteases. The tertiary structure of the Escherichia coli TdlD/TdlE complex has been solved, and shows that the TdlD subunit is the active peptidase, binding a single zinc ion at an HEXXXH motif in which the glutamic acid is a substrate-binding residue and the two histidines are zinc ligands. The third zinc ligand is a cysteine, C-terminal to the HEXXXH motif. The TldE (also known as PmbA) by itself has no catalytic activity, does not bind zinc, and does not carry the HEXXXH motif. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation.
Pssm-ID: 437122 [Multi-domain] Cd Length: 106 Bit Score: 70.72 E-value: 4.59e-15
PmbA/TldA metallopeptidase domain 1; This entry represents a group of metalloproteases. The ...
36-100
1.58e-12
PmbA/TldA metallopeptidase domain 1; This entry represents a group of metalloproteases. The tertiary structure of the Escherichia coli TdlD/TdlE complex has been solved, and shows that the TdlD subunit is the active peptidase, binding a single zinc ion at an HEXXXH motif in which the glutamic acid is a substrate-binding residue and the two histidines are zinc ligands. The third zinc ligand is a cysteine, C-terminal to the HEXXXH motif. The TldE (also known as PmbA) by itself has no catalytic activity, does not bind zinc, and does not carry the HEXXXH motif. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation.
Pssm-ID: 426306 [Multi-domain] Cd Length: 65 Bit Score: 62.27 E-value: 1.58e-12
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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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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