ID M1DUG5_SOLTU Unreviewed; 747 AA.
AC M1DUG5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 Name=102595368 {ECO:0000313|EnsemblPlants:PGSC0003DMT400094600};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400094600, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400094600}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400094600};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR RefSeq; XP_006358840.1; XM_006358778.2.
DR AlphaFoldDB; M1DUG5; -.
DR MEROPS; S08.006; -.
DR PaxDb; 4113-PGSC0003DMT400094600; -.
DR EnsemblPlants; PGSC0003DMT400094600; PGSC0003DMT400094600; PGSC0003DMG400044171.
DR GeneID; 102595368; -.
DR Gramene; PGSC0003DMT400094600; PGSC0003DMT400094600; PGSC0003DMG400044171.
DR KEGG; sot:102595368; -.
DR eggNOG; ENOG502QPQR; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; M1DUG5; -.
DR OMA; IMANEFP; -.
DR OrthoDB; 766767at2759; -.
DR Proteomes; UP000011115; 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 CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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:UP000011115};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..747
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004013869"
FT DOMAIN 26..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 137..568
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 385..451
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 646..743
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 532
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 747 AA; 79490 MW; 2D68CDD3C38A281A CRC64;
MGFFKILLVF IFCSFPWPTI QSGLETYIVH VESPESLIST QSSLTDLDSY YLSFLPKTTT
AISSRGNEEA ATMIYSYHNV MKGFAARLTA EQVKEMEKKH GFVSAQKQRI LSLDTTHTPS
FLGLQQNMGI WKDSNYGKGV IIGVIDTGIL PDHPSFSDVG MPPPPAKWKG VCESNFINKC
NNKLIGARSY KRGNGSPIDG NGHGTHTAST AAGAFVKGAN VYGNANGTAV GVAPLAHIAV
YKVCSSDGGC SDSDILAAMD SAIDDGVDVL SISLGGSPNS FYDDPIALGA YSATARGILV
SCSAGNRGPL LASVGNAAPW ILTVGASTID RKMKATVKLG NREEFEGESA YHPKISNSTF
FTLFDAAKHA KDQSETPYCK PGSLNDPVIR GKIVLCLAGG GVSSVAKGQV VKDAGGVGMI
VIKTSQYGVT KSADAHVLPA LDVSDADGLR IRAYTNSTIN SVATITFQGT IIGDKNAPIV
AAFSSRGPSR ASPGILKPDI IGPGVNILAA WPTSVDDNKN TKSTFNIISG TSMSCPHLSG
VAALLKSSHP DWSPAVIKSA IMTTADTLNL ANSPILDERL LRADIFAMGA GHVNPSRAND
PGLVYDTPFE DYVPYFCGLN YTNREVGKML QRQVNCLKVK SIPEAQLNYP SFSIFRLGST
PQTYTRTVTN VGDATSSYEV EVASPKGVVV EVKPTELNFS ELNQKLTYQV TFSKTTNNSN
FVIVGGFLKW TSNRHSVRSP IAIVLDK
//
