Family C75
Summary for family C75
Family type peptidase | C75.001 - AgrB peptidase (Staphylococcus aureus), MEROPS Accession MER0043287 (peptidase unit: 1-189) |
Content of family | Peptidase family C75 contains endopeptidases. |
History |
Identifier created: MEROPS 8.0 (8 January 2008) The operon of the accessory gene regulator (agr) of Staphylococcus aureus encodes four genes (agrA, B, C, and D) whose products compose a quorum sensing system. AgrA and AgrC resemble a two-component signal-transduction system of which AgrC is a sensor kinase and AgrA is a response regulator. AgrD is a polypeptide that is integrated into the cytoplasmic membrane via its N-terminal region, and is the precursor for an autoinducing peptide (AIP) that is the ligand for AgrC. Zhang et al. (2002) speculated that AgrB is a proteolytic enzyme responsible for the processing of AgrD to liberate the AIP, and this has been confirmed by later work (Qiu et al. (2005); Kavanaugh et al., 2007). |
Catalytic type | Cysteine |
Active site residues | H77 C84 |
Active site | The catalytic residues identified in Staphylococcus aureus AgrB by Qiu et al. (2005) are His77 and Cys84. |
Activities and specificities | The AIP is derived from the central region of the AgrD sequence, so the processing involves removal of both N-terminal and C-terminal extensions. AgrB cleaves off the C-terminus, and the N-terminus is cleaved by the signal peptidase, SpsB (S26.016) (Kavanaugh et al., 2007). |
Inhibitors | Inhibition was observed with several peptidyl chloromethanes, but not E64 (Qiu et al., 2005). |
Molecular structure | AgrB is an integral membrane protein. No three-dimensional structure is available, but the way in which it may be inserted into the bacterial membrane has been described by Zhang & Ji (2004). This model places the active site residues in or close to the cytoplasm. |
Clan | unassigned |
Distribution of family
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