ID B5Y6Q5_COPPD Unreviewed; 1851 AA.
AC B5Y6Q5;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=COPRO5265_0081 {ECO:0000313|EMBL:ACI16946.1};
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS BT).
OC Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC Coprothermobacteraceae; Coprothermobacter.
OX NCBI_TaxID=309798 {ECO:0000313|EMBL:ACI16946.1, ECO:0000313|Proteomes:UP000001732};
RN [1] {ECO:0000313|Proteomes:UP000001732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC {ECO:0000313|Proteomes:UP000001732};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus strain
RT ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI16946.1, ECO:0000313|Proteomes:UP000001732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC {ECO:0000313|Proteomes:UP000001732};
RX PubMed=24831154;
RA Alexiev A., Coil D.A., Badger J.H., Enticknap J., Ward N., Robb F.T.,
RA Eisen J.A.;
RT "Complete Genome Sequence of Coprothermobacter proteolyticus DSM 5265.";
RL Genome Announc. 2:e00470-14(2014).
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}.
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DR EMBL; CP001145; ACI16946.1; -; Genomic_DNA.
DR STRING; 309798.COPRO5265_0081; -.
DR KEGG; cpo:COPRO5265_0081; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_236872_0_0_9; -.
DR Proteomes; UP000001732; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04818; PA_subtilisin_1; 1.
DR Gene3D; 2.60.40.4070; -; 1.
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; 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; IPR022409; PKD/Chitinase_dom.
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 PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00089; PKD; 3.
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:UP000001732};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1851
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002838447"
FT DOMAIN 1424..1499
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT DOMAIN 1535..1599
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT DOMAIN 1635..1699
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 617
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1851 AA; 197717 MW; C52D61374967DB5E CRC64;
MVSNVKKTIS LILALVLIVT VLPLNVFAET PSASNAVNFG DLDQVKDQVI ETIKNNAEKA
NVPVDTVDIG GGFVISKDVY EGIKALGGKA KVIVEVNQAS FFDSWDTNLN AFKNEADKVH
AEALNQVKSA VPNFVKQYDL YATLNGFTGV VTLDQLKDIL SLAGKGRIAQ VYISKPYHVD
TVGEPISYES MQEIGVTPDM VNSAPLIGAP EAWNLGYTGA GTYVAVIDTG IDYTHENFGG
YSSFPNAKIP YGYDFADGDN DPMDHNGHGT HVSGTIGGIG KAKFKDKDGN LVPLKGVAPD
AKIIICKVFS DYGPYAYSAD IVAAIEYLIQ LKQNGVNVVA ANMSLGSDKG FDDPTDPEQK
AIKNGYLAGI TFAISAGNEA YFEYALGPNY IGANAEGKYT SYIKDPARVG APGASRYAIT
VAAVNNQGTV LQGQKLSFNN DYVMYLTSSE SPDPVAVFKK QPITIVDTNS LLCEVPQGDF
KGKVLLGDRG TCTFEVKVNN ARAAGASGVI IGNNDADASL VSMALGSAAG TIPAVFIGGP
DKLKLRSAIS AAGGSLQGVF SDEIATGYAA TNPNGMASFT SWGPAPNMAF KPTVAAPGVA
IFSSTPGNQY ATMQGTSMAA PHVAGAIAVI KQAHPDWTPE QIKQALVNTA EPISKYSPRV
QGEGRINVAK AVKNNVFITY NNQPYGELGA LTGNKTITLT ITNKGSTTYT ANITGYVTTS
LEQIVYGNQG ATYTVGSIST PASVTVNPGA TKTIHVTIQP STSWSNVFIE GRLLFTSSDG
TRVFPFLGYF GNWSLYSDKD TINGDSKWPD NNNIIDLPWW NADTWEGLTG VYYPYGGRLY
YIGRKGGQFE PKALAISAGS DYSTWNDSLV VGLGMLRNAR ALTIYVLDSA GKVVKTIVSE
NFVRAAVNSS DSTTAGLRTG WSKLWEWDGT DRNGNFVPEG QYTIRIVAMP DPLISDEANL
LPTQVMDIPV KVDKTPPTIE VSRLENAVTS SQDRDGSVIV PTASVFSLVV TGTDESSILT
YYFGEEWIPA GSDPLNTAII ELPVLETVRQ ISGTTDVDDG TILAFEIDAD DGAGNITYPD
NTITVNFAYD NPHTALELEN FEAIADGKYL KVGFDVLNAP GATYQMTIKD GNGSVVHTAT
GVVTGLDTVS HQEVKYEITK GGQYTVELTV TDIYGNSASE DGTVSFLSPI ISILPDVTFM
VVKQGTSTGI AVSVEGTAST GTVSLNRITV EDGEVKTTVV KAVAFDGRTF NDTEFIDSTL
DAGRYQVNVE VESMFGQVFA NSRRVVIDGH APALDDVKVV SDVGSITYKS EFSDNTVDVS
VRTDEDTTGQ LILKISDDYT YFDVYLDDDH IGGWGDTGVG GEGTFFVPVN LDIGLEDTYE
LRLLDEAGNE STYTINLRVM SKMITDVKLE VEGQEIYPEH GGTYTVISAP PVSGTLTFGL
SEDYEIESVS VMVNETEVAT ESPATLTFTQ AGEYTIQIRA EDNLGEKETF EFTLEVIEDR
PPEIQNVTLE SAGRVLELAD GGEYEITLPL PVEGVLTFEA SDDDEVASIS VKLNGEEVAT
ESPATLTFEE AGEYAIEITA VDSAGQITTF TSTLRVIEDV PAIIENVMLV IDDETIEPVN
GGEYEITLPL PAEGLLTFDV SDDVDVASTS VKLNGTEVGN SSPVTLNFTA AGTYVVQIVA
VDSAGQTSTF EFTLNVVEEI ISTSFELKLE AGLNYFGLPI YVDKTLGEIL PGAKVYRRSG
TSWVLATSEK PMAYAVYRVS LTEAKTVELV GEPFEPSSFT LKRNTSNYIS IPQMSPVNAN
DLFGGALTSI SVITTGGTMV KVTDGVMLPG KAYVVVVSKD VTINLPSLMP R
//
