ID E5WH41_9BACI Unreviewed; 1148 AA.
AC E5WH41;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=HMPREF1013_01746 {ECO:0000313|EMBL:EFV78061.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV78061.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV78061.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV78061.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-2010) 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:EFV78061.1}.
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DR EMBL; ACWD01000025; EFV78061.1; -; Genomic_DNA.
DR AlphaFoldDB; E5WH41; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_007528_0_0_9; -.
DR Proteomes; UP000003283; Unassembled WGS sequence.
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 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; 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 Cell wall {ECO:0000256|ARBA:ARBA00022512};
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:UP000003283};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 140..390
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 708..794
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 181
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1148 AA; 123821 MW; C726A3E2514E77CC CRC64;
MSFLIRLCHI WLPDFLDQDL FNITALIKDG YDDENQKELP VIIQYSESKG RSAVAHPIPK
GSKKTHVLES IDSVAVTADK KETKGFWKEI TKANKTPKKS KAALAPGIEK IWLDGRVEAS
LEQSVPQIGA PSAWESGYDG TGVKVAVLDT GIDPEHPDIA GQLDEAVSFV PGEEVTDMHA
HGTHVASTVL GTGEASEGRN QGVAPGSRLL VGKVLSNEGF GQDSWIIDGM EWAAENAKIV
NMSLGSSEPS DGTDPMAQAV NNLSKETGSL FVIAAGNTGS EGIGSPGAAD DALTVGAVDK
SDNLAWFSSK GPSFGSSGLK PDLTAPGVGI MAARSQYTNQ GSGSYMSMDG TSMATPHVAG
AAALLSQRHP EWTGEQLKEA LMSTTRKLED ISPFEGGTGR LDAEAAVLGN IRATGSLDFG
FYDWPHENDV PAEKTITYTN DSGQDVTLDL SISMKDSHDT DAPAGMVKLS SEKVTVPANG
IAEVTVTLDP NNGDFGSRYQ GHISASAEGQ KIVHTSLGMI KEDERYPLTI KAVDRDGEAA
SAYFYLLGPT GDPQFMSVEG TKELRLPKGT YSVMSMMDVD ADTDHAGVAL VGDPEINLDG
PQTVMLDARK ANEITVDVPK ETEANYRKME YYRSINGNDV NDIYILPVLV DKMYAAPTEK
VNVGEFTQAT RWRLAEPMLT IGYKGKELDD IPQAGSTLLN GKYNLKAVYA GNGSPEDYEN
LDVKGKAAIV QRSDELTGSE RAAAALAAGA KLLITVNDGP QELSEWVGIE NEDFSLSNSP
LPVAGISSTE GKELIAAAKS GKLTLKVEGT PDSDYLYDLV DMHHQAVPKE VNYSPKSKDL
VKINSEYKSD CPAPGAEFRY DILAHSFAGV GFLQTLSLPS VRTEWVSAQK GTSWYHQAGV
LDAQWEVRQP KVDYKPGQTL NEEWFSPVVR PRFGDGFWAP YRSGNNLILN VPAWADSGPG
HTGADMNYPG DQTLKLYQGD NLVKEGKGQA LYLFNEFPEE KTQYKLVSDA ARDAERWNTS
VRTHTEWTFW SQKQGEFQTA LPLISIDYKV DTDMSGNSTA GKKIKLDLSA VQITDAPENG
QIKGAALEVS FDEGKTWEAA KLVSKGNGWS AEIKHPNKKG TSVSLRASAW DDAGNRVNQE
IIKAYGLK
//
