ID V8BCW8_STRPA Unreviewed; 1498 AA.
AC V8BCW8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=HMPREF1195_01148 {ECO:0000313|EMBL:ETD13014.1};
OS Streptococcus parasanguinis CC87K.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1073372 {ECO:0000313|EMBL:ETD13014.1, ECO:0000313|Proteomes:UP000018716};
RN [1] {ECO:0000313|EMBL:ETD13014.1, ECO:0000313|Proteomes:UP000018716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC87K {ECO:0000313|EMBL:ETD13014.1,
RC ECO:0000313|Proteomes:UP000018716};
RG The Broad Institute Genomics Platform;
RA Earl A., Allen-Vercoe E., Daigneault M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Streptococcus parasanguinis CC87K.";
RL Submitted (OCT-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:ETD13014.1}.
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DR EMBL; AZJD01000004; ETD13014.1; -; Genomic_DNA.
DR RefSeq; WP_023919023.1; NZ_KI669401.1.
DR PATRIC; fig|1073372.3.peg.1179; -.
DR HOGENOM; CLU_001768_4_1_9; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000018716; 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; cd07475; Peptidases_S8_C5a_Peptidase; 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; IPR034216; C5a_Peptidase.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR019931; LPXTG_anchor.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; NF040553; SGO_0316_fam; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04650; YSIRK_signal; 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; 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}; Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 5..29
FT /note="YSIRK Gram-positive signal peptide"
FT /evidence="ECO:0000259|Pfam:PF04650"
FT DOMAIN 280..739
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 555..623
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 777..887
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT DOMAIN 1462..1497
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 54..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 692
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1498 AA; 164041 MW; D5A010D18CD978BD CRC64;
MEFHRQQRFS IRKYAIGVAS VLIGTFLMGS AVSADTIVPT PSVVEPSVVV PETAATDEKT
AEPLSATKDS MPTSVIEDTA SKNLATAEIE SKEKTNQSLP SSSIDTSSSA TNQVEAEKAS
PSVAEAPKEN GVATPITTSI EPVKENLEET SPVEVLVRLK EKVSEGIGEV SPTSKETRIE
KTNQDHEQFL KELEKQSIQF KKLYDFNLLF NGLALETTYG DAKKIRGLAR VDAVDYAPLG
RTRVAETQPT PASPTSTTTK VSEENSLINL QPLWDKGIKG QGQVVAIIDS GVDPAHDVFR
LTDISKAKYK SEAEIEEAKK KAGITYGKWY NNKIVYIHNY SDMDDNVKED DPISHGAHVA
GTAVGNASQP SPNGEIIRGV APEAQLMFLR VFSDTKGGQV QNFIYTKAVE DAVKLGADSI
NMSLGTASSS VYDVGEITRQ AFDTARKAGV TITVASTNMA TNGFWHSKPL ATTPDYGMTG
TPSVNPNVIS VASINSLTKH ESTEASLTVD ALKDSKDFPE GKIPMHSFVE RDAFRTTIPQ
SYLHVEKGGI DHYQADSING HLVLTERGGE VSDVDKVKEL KRAGATGVIF YQTKEQGNNP
VSFDLEGLGE RFPVGVIGHA AGLVLAQHAN DYQLHIANKF KRVPYDAANQ LSDFSSWGLS
ADGDLKPDVT LPGGMIYSSV NNGEYYMDRG TSMASPHAAG ATALVKQALK ERFPHLSPEQ
LQVLVKQMTM STAIPHVDEE THAYSSVRQQ GAGVMDVTAA ALGDLYVTAK DAKSSLTLGN
VTDTFEFDVT IHNLSNQDKS VRYETTLQTD QVQDGKFTLH PRLLETLDGK ETVTIPANGQ
RTIHVAVDAS KYKEELSKQM PNGYFLEGFV LVKDASTQKH LVSLPYVGFH GDYQNLRGIE
KPIYEYTGSY KPFYYYKDKT DYPDEKVPET PERHPDNHFT SLISYVYENG ESVAKTLGQD
GDRFDGDQLY FSPNNDSSFD SIKVKAVMLR NVENVHLSVY KKEDTARTNP IYEVGNEVHR
KTDWSYRIGN RSEEFYEISW EGLDKDGKQL PDGEYQFVIT YRPTASGAKQ QELNFKVKID
NTAPSIESGS AQYDPATRIF RPGKVLETGS GLAGTYLSYV KDGETVALEP QEDGSYLLPE
GVDPSTVRYT IWDKVYNTIE MDIEGKKVEA TTPTNEAGSD EQPSETASEK LKAEKGTLEV
VFTDSSGEVI SYYPSVVRYQ VVDDQGRVVE GEFNVSYNGG TFPDLPFGTY TAKITLSDYH
YDWGTELVKK VTVSPENPHP KVTFAFHYLD ENKLTIGFDQ PVPAGTVVKV VGNDGISRLL
PQSIYDLLRF ETMLMNGSYR VHVDLPAGYH VSENDFLYEV SNRINYHLLS LVKDVIKPNP
EVHSGAIVEP WIQPENPTLV IDEVPSRHSE TPVTPDQLAV SKGPVTPAQP AAIETKEVAT
NKPVAVTYHT SGQAEVAATP ATGLPKTGQD ELASTVLSLF GMTSLALAGF VASKKREG
//
