ID A0A2H3KGV5_9CHLR Unreviewed; 1124 AA.
AC A0A2H3KGV5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=A9Q02_05380 {ECO:0000313|EMBL:PDV96973.1};
OS Candidatus Chloroploca asiatica.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Candidatus Chloroploca.
OX NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDV96973.1, ECO:0000313|Proteomes:UP000220922};
RN [1] {ECO:0000313|EMBL:PDV96973.1, ECO:0000313|Proteomes:UP000220922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7-9 {ECO:0000313|EMBL:PDV96973.1,
RC ECO:0000313|Proteomes:UP000220922};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:PDV96973.1}.
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DR EMBL; LYXE01000170; PDV96973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3KGV5; -.
DR OrthoDB; 9762689at2; -.
DR Proteomes; UP000220922; 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; 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; 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:UP000220922};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 212..673
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 484..571
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 639
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1124 AA; 116638 MW; 551EF9C030B4E630 CRC64;
MVGRGRWLLV TLALTMLVSG FAFTFAQSNL GSGSFTAAPE RIVPVSEVDL DAFLYERVSP
EDAALIAGLV ARDRIAPRGA VIPAAQRGED TTIPTLEALG DEVIDVVVYL DMPALVEQVS
ISAAQRTAYA NRIAQVQTRV GSEIEALGGT VIHRFTTLSS GIAVQMPANL AGRVSRIAGV
ERLSHVRNYT RDLTETVPFI GASTLQSLDV TGAGVKVAVI DSGIDFSHLA FGGPGTEAGW
EAAYYGDSPD CDRAAAHDPD CAYAQPADPA LFGPAAPRIK GGFDWLGEQW NGSTNTTIIT
DSNPIDFEGH GTHVADIIGG LGYPAGTNED GAYPAKGVGV APEAEIYGFK ACASFSSACN
GLALLASVDN AADLDRDPAT VDPVDVINMS LGSPYGQPED DLTYFSNRAA GMGIIVVASA
GNSADKPFIV GSPSMGDGVL SVAQTAVPSA TRYPLFYASS TVSGTINAAV FQNWSVPPPN
VLIQGSVVYG NPDGSNTNGC APYTTPLTGS VVLADRGGCF FTLKAVNASA AGAAISLIGL
IAPGDPSEFG DGGDRPITIP SFVISQAASN LLKAQIANSV VAGVDPADAI NLANTIVGSS
SRGPRNHDNV IKPDIGAPGA SISAIAAGGA ATGPFGGTSG AAPMVSGVAA LLKQVYTDTL
IVQQYKALLM NTGNLEIWQG DPGTVLAPIT RIGGGQVDAS AAYSSTLVAW DSTSASSLAW
TGSMSFGYQP VAANQTLTRT LTIKNLANAA QTVTLASVFR YAQDADQGVV VTPGQSEVTI
PANGTVDVPV VMTIDPATLH PWVVNKGSLG ANGAALTFQE YDGHVTITPT SGAPIHVVWH
VLPKAAADVS LSATNWLSET TMLNNAAAAI TGTVDIFDLI VADANDYGFT VGDCASVGFE
PGCNTTIVDL KEIGVRTTTA VSPSDFLEFA VTLWDEPYRA SQYPVEIDIY IDANNDGTDD
YVIFNADLAL NGSDGRNVVF VVDLSDNSLF PAYFIDSTFN TQNFILPMDA ASIGITPGQP
FSFSVFAFDA YFGGLWDCAP KVNGVCSGSY QYTPGLSRYA IPEADRFVDV PPAGSVNVAW
TSSPEGAAAS PSQTGLLFMY RNALVGRESD RVLKINTYLP FIQQ
//
