ID A0A1I1FNV9_9GAMM Unreviewed; 458 AA.
AC A0A1I1FNV9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=C5a peptidase {ECO:0000256|ARBA:ARBA00020956};
DE EC=3.4.21.110 {ECO:0000256|ARBA:ARBA00012942};
DE AltName: Full=SCP {ECO:0000256|ARBA:ARBA00030432};
GN ORFNames=SAMN02745724_00699 {ECO:0000313|EMBL:SFC00686.1};
OS Pseudoalteromonas denitrificans DSM 6059.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1123010 {ECO:0000313|EMBL:SFC00686.1, ECO:0000313|Proteomes:UP000198862};
RN [1] {ECO:0000313|EMBL:SFC00686.1, ECO:0000313|Proteomes:UP000198862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6059 {ECO:0000313|EMBL:SFC00686.1,
RC ECO:0000313|Proteomes:UP000198862};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This virulence factor of S.pyogenes specifically cleaves the
CC human serum chemotaxin C5a at '68-Lys-|-Asp-69' bond near its C-
CC terminus, destroying its ability to serve as a chemoattractant.
CC {ECO:0000256|ARBA:ARBA00002909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The primary cleavage site is at 67-His-|-Lys-68 in human C5a
CC with a minor secondary cleavage site at 58-Ala-|-Ser-59.;
CC EC=3.4.21.110; Evidence={ECO:0000256|ARBA:ARBA00001404};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; FOLO01000003; SFC00686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1FNV9; -.
DR STRING; 1123010.SAMN02745724_00699; -.
DR Proteomes; UP000198862; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.120.380; -; 2.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 2.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000198862}.
FT DOMAIN 79..143
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 151..216
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 267..332
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT DOMAIN 375..442
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
SQ SEQUENCE 458 AA; 46956 MW; E942EF4668287F0B CRC64;
MSFAAIDSNK ALADFSQKNN PVEISGPGVD VYSTYPDGLG SVIEVSVAGV SYTANAMENK
GSASGTLYNL GTGEAIDNGA SGRICLIQRG NISFHDKVKA CEDSGGIGAI IYNNASGAFG
GTLGDTNATT IPGVTVSDSD GATMLANLDS STSINIGAGN YGKKSGTSMA SPHVAGVAAL
VWSHHPSCTN VEIRNVLNST AQDLGAAGRD VKFGYGLVQT KDAIDSITAN GCDGNGTGPV
EPPVGNNVLE NGVAATGLEA ITGSDVVYTM EVPAGATKIS FSMSGGSGDA DMYVKFGSAP
TDSSYDCRPF ENGNTESCTV TQTAGTYHVR IKAYSGFSGV SLTGSYTADS GNGGIVQPVN
ETINDVSVSR RSWTRYTFDL AEGYADLNVA ISGGTGDADL YVTQGRQSTS SSYDCRPFEN
GNSESCAFTT PTAGKWYIDI YGYSAASGMT LKLEATPK
//
