ID U1Q5S8_9ACTO Unreviewed; 1025 AA.
AC U1Q5S8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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};
DE Flags: Fragment;
GN ORFNames=HMPREF1980_02202 {ECO:0000313|EMBL:ERH23240.1};
OS Actinomyces sp. oral taxon 172 str. F0311.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1321775 {ECO:0000313|EMBL:ERH23240.1, ECO:0000313|Proteomes:UP000016501};
RN [1] {ECO:0000313|EMBL:ERH23240.1, ECO:0000313|Proteomes:UP000016501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0311 {ECO:0000313|EMBL:ERH23240.1,
RC ECO:0000313|Proteomes:UP000016501};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERH23240.1}.
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DR EMBL; AWSF01000223; ERH23240.1; -; Genomic_DNA.
DR AlphaFoldDB; U1Q5S8; -.
DR STRING; 1321775.HMPREF1980_02202; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_006694_0_0_11; -.
DR Proteomes; UP000016501; 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 Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 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 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}; 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1025
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004618241"
FT DOMAIN 188..657
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 456..526
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 693..809
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 592
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1025
FT /evidence="ECO:0000313|EMBL:ERH23240.1"
SQ SEQUENCE 1025 AA; 106941 MW; 402E8E6D2FEF0D4D CRC64;
MKKPAVLLAF VGACALAVTG PASVASPLVS GERPATKTAA SSLPVGDLDT ALTSKSGQSH
DAESDTDRDP ARVVGIIVQL EDGADAAASL ASINEAVAGA FPGAQVQVQR EYDNALVGFA
LRAPAGSLDA IRASSGVRAA FLEREGRVSD VAAMDAEGGT RASQVEGQDP ANLSAQLMMR
TDQVTQKGEG KVIAVIDTGV DMTHPAFTGA MPDNVALSED QVQALVPHLG AGKSGQYMSE
KFPFAYDYAD DDVDAAPREG GSGFHGTHVA GIAAGNADKI VGTAPDAQII VGKVTRSEDD
ALLDSSLLAA LDDMVVLHPD VINLSLGWTA GMDNEADSVY DTVYKKLQEE GITVNAAAGN
AFSTGYGNNS GKGLPYASDP DTSVMDEPAT YPSVVAVGSV ENALIRNAFT AAGMDIGYQR
SRGMNGEKVA YFSDLPAGTY EYVDAGFASE EDVAALKEKF PNGLSGKIAL VSRGKMTYQK
KVENLYDLHP AGVIVYNNVS VGSLIIMNLT TQDVPAAFIS QADGQAMLAA SDHHLTIAEG
QVLPQSTTYE ASEFSSWGVS PDLRLKPEIA APGGNVFSAI PNGAYEQTSG TSMATPQMAG
ISAIVLQRVQ SDPLFASMSA RDKADVVQNL IMGTARPLTD AAQTSGALYS PRKQGAGLVD
ALAATTSSVY PTVAGAAEPS RPKADLGDGT TGWHFDVTLR NLGAAPATYE LSSQALSEIV
DGGFFTEHSS DWRGRGVEVT YSGAASASAE GATVTVPALD EATVGVDVMP GSVFASYVAD
NTPNGTFLDG FVRFASKTDG QPDLAVPYLG FYGDWGKAPI FDALASTGGA HTRASEIVNG
STGDSLGYNP LIKVADRTGK PNPQRYVISR SAASGAPTVL EPRTGTLRSV HALTSTYTNE
AGETVFSVTN HRNWKSIYLT STEQNTWVEA YHDSTAFDAN AEKFARMPDG AYKLTIAAQG
DGPSRTEQSI SYDFLLDTAA PVISELVYSG KDEGFVVTFD VTDDSPLAAV DLHDPADGLW
FYRHV
//
