ID H3NBU8_9LACT Unreviewed; 1729 AA.
AC H3NBU8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=HMPREF9703_00029 {ECO:0000313|EMBL:EHR35181.1};
OS Dolosigranulum pigrum ATCC 51524.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Dolosigranulum.
OX NCBI_TaxID=883103 {ECO:0000313|EMBL:EHR35181.1, ECO:0000313|Proteomes:UP000003599};
RN [1] {ECO:0000313|EMBL:EHR35181.1, ECO:0000313|Proteomes:UP000003599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51524 {ECO:0000313|EMBL:EHR35181.1,
RC ECO:0000313|Proteomes:UP000003599};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dolosigranulum pigrum ATCC 51524.";
RL Submitted (JAN-2012) 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:EHR35181.1}.
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DR EMBL; AGEF01000001; EHR35181.1; -; Genomic_DNA.
DR RefSeq; WP_004634535.1; NZ_JH601103.1.
DR STRING; 29394.BWX42_01140; -.
DR PATRIC; fig|883103.3.peg.28; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_001768_4_1_9; -.
DR Proteomes; UP000003599; 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; cd02133; PA_C5a_like; 1.
DR CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 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; 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; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000003599};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 186..671
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 466..542
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 694..807
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 81..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 610
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1729 AA; 190783 MW; F8AEE8C887B20277 CRC64;
MKLLRKKNGQ WFTVSVAVGM LMALGNVSQE VSAHETLPEV SDVLEQGEIV EAAGQDANVE
REQVVTETEQ SVSELENYAE IADDSVEAES ITTEKGHESS EKTAEVEQRD ASEHTVKDAS
REERSTELEG KNQSKVNKPS ENSTELDYVL PQEAVQGGAE DQHHPQAENS NQIIHAPQAW
QAGYRGEGEV VAIIDSGIDP VHDAFGRLSD MMKARYQTQE QFEKAKLAAG IEYGRWVNEK
LIFGYNYTDA DIHLKENDLM SHGQHVAGTA VGNPSRPVKL PTLDNPDNEE YIYGVAPEAQ
LMAMRVFSDL NGGTWEYLYA RAIEDAVKLG ATSINLSLGG GSGSLYETSY RLSKAIADAN
AAGVSVVIAA GNSRVFGQGH SNPKASNPDI GVVGSPSTAQ NSISVASVNS TVAMEYVLQV
KGLEKAEFNH GNLMVGFGDN KSQEILRQPE FAEGEFEYEV AGLGKEADFA GRDLSGKFAL
VKRGEISFED KALHAKRAGA KGIVVYNRDD SDDEVMTMTL GDNPELKDFP ALFITNRAGN
ELAAHADKYR LKPDTQHRMK FDHPNKGEMS YFSSWGLSAD GELKPDVTAP GGGIFSAYND
GEYGPMSGTS MASPHVAGAV ALIKQGLRKK YPEMSAGELT ALVKNLLMST ATIHTNPETG
AFTSPRQQGA GIINVDKALT SDLYVTNNKG YGSVSLYNVG DQLRFDVVVH NRSNEAKTLT
YQTHLNTDAT KDSPIGPLMS LQPRHLKTTE RQTVTVEAGE SKTISITVDA SEFSEELLTQ
MKSGYFLEGY VVFKDEAGQG LVNIPYVGFR GDFSSLRVVE TPIYDLEKGE VPFYYYANVE
EQVVDPHEDH FTSLVTAVDT GKDKPQIQTL GADTVDPEGN FLEQGKDMKL ALSPNGDGHK
DELGFKGVFL RNYEDFVASI YALDDVSREK VLWRSEKTSG RKNYFDGQDD KSTLVPESVW
NGLDYLGNLL ADGQYKYVVN YRPVVPGADL QELTFDLTLD TQLTMATAAD FDAQLRKLTF
RNTNELASDL SGINPFRTSI GYKDGSPLAE GLPRLYMNED LTFDIPEGVD ITDKRLVLNL
EDNAGNRKQK KLNELLIGMT GVVNFRLLDE VTGENYAKYG FRVLIRDEAG NIVETIEHAG
KKGSTLRLPF GTYTAETFLY DIEYLEVVGN IQKTFTVSFE QSVQTVDFLA KQTIYREFRV
QLNESLPQGA TVYAVDAAGK RYLVPTTSYH PDRLQVRLPE GTYTIVVELP AGYSSEQNGA
VVELTENSST FHLAIEQIEV APAVDLNPFV DELLNINQHI EAEEQVDKGA FLNKWLEKTK
ETEEQPEEEP EVSSEPEQQP EGTVQEQLED SQVLAKKKVE ANLAIIRSEQ ASDNLKQTYL
TLIRQADGVE AVQALLAEFQ QKATVEDTTV PTPPQEPEEI PEPGLKTIKN HFKLVVDFDG
EQVVYDRKDS DVWASEEHAR EVYDQYLPEV IERDGKEYER INITFKQLAE EAILTYVFKL
KTDLTVAVAP PAEENESVQE TEKPVQPERP EIEKNQSTGK VIDSTDDNQL PDDSNIETGK
GLIRPDKPAF EGGVNHHKAA IHEKTMFPDH QLQALLQVEK NKAKTYIATL SDLTATSTMT
YQEAIQQANN VPTIEQIIRQ AVTVNEQLTV QAAMNEITDQ KNKSNETHIL LQTVSITDRT
SQSANKQLAE KATEGERLPD TATSSWIIGL VGVSSLLAGV SVKKLKNDK
//
