ID G4TJN6_SERID Unreviewed; 965 AA.
AC G4TJN6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=PIIN_05468 {ECO:0000313|EMBL:CCA71532.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA71532.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA71532.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA71532.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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, ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCA71532.1}.
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DR EMBL; CAFZ01000123; CCA71532.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TJN6; -.
DR STRING; 1109443.G4TJN6; -.
DR eggNOG; KOG4266; Eukaryota.
DR HOGENOM; CLU_003559_3_1_1; -.
DR InParanoid; G4TJN6; -.
DR OMA; FNHPALG; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000007148; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02124; PA_PoS1_like; 1.
DR CDD; cd07489; Peptidases_S8_5; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034187; Peptidases_S8_5.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..965
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003468590"
FT DOMAIN 169..593
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 400..453
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 638..740
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 927..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 550
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 965 AA; 100846 MW; 7AD3752E0CB640F5 CRC64;
MRAAACIAFV CALSLHLFNP PTLVSASSLD RRDGIPSAAA DAENIVPGKY IIELDSPAAG
SKHKRSLTPH QDFYDELARR GISVETGIEF NDPNLFVGLE VSVGNSADLD VILSMQRVVA
IRQVLMMAIP PLVKYQPVNG VNDPALPPDT QSTHVMTGVD KLHAQGNFGQ GIQIGIIDSG
IDYLNPSLGG GIGSNFLVKG GYDFVGDAYT GGNTPVPDDD PMDTHRGAQF SVESRACYGH
GTHVAGIIAA QPGNIYNITG VAYKSSIYAY RVLGCTGTAQ DPVVVEALLR AYRDGNDVIT
LSLSSGSGWS TSTTGVVASR IAKKGRVVTA SLTNDGQMGA WNTPAPASGD DVIAVGSVEN
SVLPSINVTL SDGHAPIPYF SLRAFPVSGS LPVYATSTDV TITNDACNPL PANTPNLAGY
LVVIRRGGCS VATKFANAAA KGAKYFFLYN DGSALGIISS GGYIAVLIRA EDGVYLVNSF
ASGANVKVTF SPSTAPGFTE IPGGGLISTY SGMGPTYDLR IKPAVVAPGG NILSTIPRAF
GGWGVSSGTS MATPFVAGSA ALYLSARGKG DKTARSVKKA LQNTAMMVPA STADGAPYVS
VAQQGAGLIN VYNAIHARTV VSTSELLLND TAYGNNVQII TLSNPTKKSV TYTVSHTPGL
TISTINSATK LPYTSPLPTS SQAASVSILS QKFTVWPGFF NGFILSIQPP AGVDPKTFPI
YSGFVTISSS LGETFSIPYL GVAAKMKDMA ILDRTAQSFG IQLPALLDSA GKVPKPNQTF
SLIGNDYPAI LYRRAAGTPS FLADLVMPNT QVPGVTPAAK KRGLFWNWLN GIFGNNNGRI
TVPSGSFFNV PTVGPVQSFP YKPRHIVASD EGNGYDWVRV TSFLNRTAIP NGTYRLLIRS
LKVTGNRNVE EDYDAWLSPV FTIGTPSNST TTTSTSTPLS TSTSASTSSS TSTPVSSTSS
STVSV
//
