Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APmbA_TldD_3rde5njaA3 A: beta barrelsX: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)H: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)T: barrel domain in putative modulator of DNA gyrase, PmbA/TldDF: PmbA_TldD_3rdECOD (1.6)
APmbA_TldD_2nde5njaA1 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: PmbA_TldD_2ndECOD (1.6)
AUNK_F_TYPEe5njaA2 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: UNK_F_TYPEECOD (1.6)
CPmbA_TldD_3rde5njaC1 A: beta barrelsX: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)H: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)T: barrel domain in putative modulator of DNA gyrase, PmbA/TldDF: PmbA_TldD_3rdECOD (1.6)
CPmbA_TldD_2nde5njaC2 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: PmbA_TldD_2ndECOD (1.6)
CUNK_F_TYPEe5njaC3 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: UNK_F_TYPEECOD (1.6)
BPmbA_TldD_3rde5njaB1 A: beta barrelsX: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)H: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)T: barrel domain in putative modulator of DNA gyrase, PmbA/TldDF: PmbA_TldD_3rdECOD (1.6)
BPmbA_TldD_1ste5njaB2 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: PmbA_TldD_1stECOD (1.6)
BPmbA_TldD_2nde5njaB3 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: PmbA_TldD_2ndECOD (1.6)
DPmbA_TldD_3rde5njaD2 A: beta barrelsX: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)H: barrel domain in putative modulator of DNA gyrase, PmbA/TldD (From Topology)T: barrel domain in putative modulator of DNA gyrase, PmbA/TldDF: PmbA_TldD_3rdECOD (1.6)
DPmbA_TldD_1ste5njaD1 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: PmbA_TldD_1stECOD (1.6)
DPmbA_TldD_2nde5njaD3 A: a+b two layersX: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)H: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523) (From Topology)T: a+b domain in putative modulator of DNA gyrase, PmbA/TldD (Pfam 01523)F: PmbA_TldD_2ndECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B3.30.2290.10 Alpha Beta 2-Layer Sandwich PmbA/TldD fold PmbA/TldD superfamilyCATH (4.3.0)
D3.30.2290.10 Alpha Beta 2-Layer Sandwich PmbA/TldD fold PmbA/TldD superfamilyCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, C
PF19289PmbA/TldA metallopeptidase C-terminal domain (PmbA_TldD_3rd)PmbA/TldA metallopeptidase C-terminal domainThis 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 gl ...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 [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3].
Domain
A, C
PF19290PmbA/TldA metallopeptidase central domain (PmbA_TldD_2nd)PmbA/TldA metallopeptidase central domainThis 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 gl ...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 [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3].
Domain
A, C
PF01523PmbA/TldA metallopeptidase domain 1 (PmbA_TldD_1st)PmbA/TldA metallopeptidase domain 1This 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 gl ...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 [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3].
Domain
B, D
PF19289PmbA/TldA metallopeptidase C-terminal domain (PmbA_TldD_3rd)PmbA/TldA metallopeptidase C-terminal domainThis 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 gl ...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 [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3].
Domain
B, D
PF19290PmbA/TldA metallopeptidase central domain (PmbA_TldD_2nd)PmbA/TldA metallopeptidase central domainThis 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 gl ...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 [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3].
Domain
B, D
PF01523PmbA/TldA metallopeptidase domain 1 (PmbA_TldD_1st)PmbA/TldA metallopeptidase domain 1This 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 gl ...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 [1]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [2-3].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, C
Metalloprotease TldD
E, F
HIS-PRO-PHE
B, D
Metalloprotease PmbA

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
E, F
PharosP01019