ID A0A0X3RYK3_9ACTN Unreviewed; 1262 AA.
AC A0A0X3RYK3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ADL25_31705 {ECO:0000313|EMBL:KUJ36614.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ36614.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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, 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:KUJ36614.1}.
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DR EMBL; LMWH01000253; KUJ36614.1; -; Genomic_DNA.
DR RefSeq; WP_059131335.1; NZ_LMWH01000253.1.
DR AlphaFoldDB; A0A0X3RYK3; -.
DR Proteomes; UP000054048; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
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; IPR017296; Peptidase_S8A_SAM-P45.
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 PIRSF; PIRSF037852; Subtilisin_rel_SAV5721; 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:UP000054048};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 227..504
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 830..880
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 255..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 236
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 284
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 457
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1262 AA; 132156 MW; EBAEE86DD878CD31 CRC64;
MLSLSVTTSA GAQPVRQTGS TAAAGAPAAA AAAQPRTVTL ITGDKVTVTP AGDAGTMTVS
GPHGEPVAAH TDKVGKDLYV YPESAAPYVS AGLLDKELFN VTGLVADGYD DARVNHLPLI
VTYTHNAAAR AQAAPRGANR VRTLSSINGA ALAEDHDKAT EFWSAVTAKV SASAVSRSSE
LLVSPAPRPT LAGGISKIWL DGRAKATLAD STAQIGAPEV WRGGNTGKGV DVAVLDTGVD
DGHPDLVGQV AEATSFVPDQ PPGGGDGPQG QATADTDAVD HHGHGTHVAS TIAGTGAASG
GKEKGVAPGV RLHIGKVLND SGEGQDSWIL AGMEWAVRDA HAKVISMSLG GSPSDGSDPL
SQAVNQLSAE TGALFTIAAG NSGPDSKTVA APGAADAALT VGAVDGDDKL ADFSSRGPRW
SDSAIKPEIT APGVDILAAR SRYAGGSGDY TTMSGTSMAT PHVAGAAALL AAEHPDWTGG
QIKDALVSTS KSTPTYTAFQ AGVGRVDIAA ATKSTLYATG TVSLGEHPWP ADPGATVDKT
VTYTNIGDSA VTLDLAVSAP KAPAGLFTLS KDKVTVPAHG TSTVTVTADV DKAARGTTYD
ARIDASAEGV PLAHTAVGFV TANQTFKVTI VSKDRSGGIY TGPGTLMGAS DETSDPFVNN
WNINFDIDSP GVLTLELPAG TWSLGQWMEV EGSHGPQSRG HALVMVPQFD LNRDTTIVLS
AAKARQMKLL TPRESRSSAL RVDYTRAFPG AGNQVMSFLV PRTEDTLWAV PTAKVTKGTF
DVRTRWRNEQ PALKISVGGT SFDDLLVRRG TKPLSKGSHR LRPVYVGQGA AADYTGRDVR
GKAAVVDRND TVGLSEQAAT AASAGAALLL VVNDGPGLVE PLAFDSIAPL NIATLDREEG
RRLISQAAKS GTALEVYSNP TTEYLYDVVR NHRSQIPTDL TYRPNTGDLA RVDMSFRNYR
PAQATDFRYD VYPESDWWAI GWPEIPGQGQ GDRTDYVSPG VQYRESATVT GETRVIAADK
RYGPGSRTAE NWFSPIQRPR ISYDGTSLSR QDDALFAFVA GWGDAGADRG GYGTAPGVQA
KTSIYQGDTL LAQSSDYYTY ATGLKPEALP YRIVSEFSRG TWASPYSTRT RTVWDFTSAA
GRRYQNMPLP LVQLDYDVTT DFSGKAGRDA VFTIKPAKPS GEWPKAYADL PPAAFHDGTL
ELSYDDGVTW HRAHLTRTSD GRGWRTELNA PKGARFVTVR AGATDSDGNS VEQTIVRAFG
LK
//
