PmbA_TldD

• PFAM accession number: PF01523
• Interpro abstract (IPR002510):

  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 [ (PUBMED:28943336) ]. TldD and TldE were originally identified as regulators of DNA gyrase. Later, they are shown to be metalloproteases involved in CcdA degradation [ (PUBMED:22950735) (PUBMED:12029038) ].

• GO process: proteolysis (GO:0006508)
• GO function: metallopeptidase activity (GO:0008237)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PmbA_TldD