Domain

Colicin V processing peptidase (IPR033838)

Short name: CvaB_peptidase

Overlapping homologous superfamilies

None.

Domain relationships

Description

This entry includes the processing peptidase for the bacteriocin colicin V (MEROPS identifier C39.005) [PMID: 9106219]. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions [PMID: 7565085]. The proposed protease active site is conserved in members of this entry [PMID: 14570918].

This entry also includes the N-terminal peptidase domain of secretion/processing ATP-binding protein MchF, which processes microcin H47 and is closely related to that of colicin V [PMID: 11181394].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0008234 cysteine-type peptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
CDD