ID Q8E6V8_STRA3 Unreviewed; 1233 AA.
AC Q8E6V8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
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=gbs0451 {ECO:0000313|EMBL:CAD46095.1};
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110 {ECO:0000313|EMBL:CAD46095.1};
RN [1] {ECO:0000313|EMBL:CAD46095.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316 {ECO:0000313|EMBL:CAD46095.1};
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AL766845; CAD46095.1; -; Genomic_DNA.
DR RefSeq; WP_000357569.1; NC_004368.1.
DR AlphaFoldDB; Q8E6V8; -.
DR KEGG; san:gbs0451; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_001768_3_0_9; -.
DR Proteomes; UP000000823; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02133; PA_C5a_like; 1.
DR CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 2.60.40.4070; -; 1.
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 Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR034216; C5a_Peptidase.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR013783; Ig-like_fold.
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 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; PS50847; GRAM_POS_ANCHORING; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW 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|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1233
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004307836"
FT TRANSMEM 1204..1223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1197..1233
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 96..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 578
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1233 AA; 135763 MW; 723F5B568E578EE7 CRC64;
MDKHHSKKAI LKLTLITTSI LLMHSNQVNA EEQELKNQEQ SPVIANVAQQ PSPSVTTNIV
EKTSVTAASA SNTAKEMGDT SVKNDKTEDE LLEELSKNLD TSNLGADLEE EYPSKPETTN
NKESNVVTNA STAIAQKVPS AYEEVKPESK SSLAVFDTSK ITKLQAITQR GKGNVVAIID
TGFDINHDIF RLDSPKDDKH SFKTKAEFEE LKAKHNITYG KWVNDKIVFA HNYANNTETV
ADIAAAMKDG YGSEAKNISH GTHVAGIFVG NSKRPAINGL LLEGAAPNAQ VLLMRIPDKI
DSDKFGEAYA KAITDAVNLG AKTINMSLGK TADSLIALND KVKLALKLAS EKGVAVVVAA
GNEGAFGMDY SKPLSTNPDY GTVNSPAISE DTLSVASYES LKTISEVVET TIEGKLVKLP
IVTSKPFDKG KAYDVVYANY GAKKDFEGKD FKGKIALIER GGGLDFMTKI THATNAGVVG
IVIFNDQEKR GNFLIPYREL PVGVISKVDG ERIKNTSSQL TFNQSFEVVD SQGGNRMLEQ
SSWGVTAEGA IKPDVTASGF EIYSSTYNNQ YQTMSGTSMA SPHVAGLMTM LQSHLAEKYK
GMNLDSKKLL ELSKNILMSS ATALYSEEDK AFYSPRQQGA GVVDAEKAIQ AQYYVTGNDG
KAKINLKRVG DKFDITVTIH KLVEGVKELY YQANVATEQV NKGKFALKPQ ALLDTNWQKV
ILRDKETQVR FTIDASQFSQ KLKEQMANGY FLEGFVRFKE AKDSNQELMS IPFVGFNGDF
ANLQALETPI YKTLSKGSFY YKPNDTTHKD QLEYNESAPF ESNNYTALLT QSASWGYVDY
VKNGGELELA PESPKRIILG TFENKVEDKT IHLLERDAAN NPYFAISPNK DGNRDEITPQ
ATFLRNVKDI SAQVLDQNGN VIWQSKVLPS YRKNFHNNPK QSDGHYRMDA FQWSGLDKDG
KVVADGFYTY RLRYTPVAEG ANSQESDFKV QVSTKSPNLP LLAQFDETNR TLSLAMPKES
SYVPTYRLQL VLSHVVKDEE YGDETSYHYF HIDQEGKVTL PKTVKIGESE VAVDPKALTL
VVEDKAGNFA TVKLSDLLNK AVVSEKENAI VISNSFKYFD NLKKESMFIS KEGKVVNKNL
EEITLVKPQT TVTTQSLSKE ITKSGNEKVL TSTNNNSSRV AKIISPKHNG DSVNHTLPST
SDRATNGLFV GTLALLSSLL LYLKPKKTKN NSK
//
