SMART: Pfam domain Peptidase_C39

The domain within your query sequence starts at position 12 and ends at position 155; the E-value for the Peptidase_C39_2 domain shown below is 2.6e-9.

LPVPIIQQLYHWDCGLACSRMVLRYLGQLDDGEFENALQELQLTRSIWTIDLAYLMRHFG
VRHRFCTQTLGVDKGYKNQSFYRKHFDTEETRVNQLFAQAKACKVQVEKCGHRCFCRTPD
YQGHFIVLRGYNRATGCIFYNNPA

Peptidase_C39_2

PFAM accession number:	PF13529
Interpro abstract (IPR039564):	This entry represents a group of peptidase C39-like proteins. 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. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures [ (PUBMED:11517925) (PUBMED:14570918) ].

PFAM accession number:

PF13529

Interpro abstract (IPR039564):

This entry represents a group of peptidase C39-like proteins.

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. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures [ (PUBMED:11517925) (PUBMED:14570918) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_C39_2