ID A0A2M9JM56_9ACTN Unreviewed; 1338 AA.
AC A0A2M9JM56;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-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=CG723_31805 {ECO:0000313|EMBL:PJN07942.1};
OS Streptomyces sp. CB01635.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN07942.1, ECO:0000313|Proteomes:UP000232157};
RN [1] {ECO:0000313|Proteomes:UP000232157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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}.
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:PJN07942.1}.
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DR EMBL; NNBL01000017; PJN07942.1; -; Genomic_DNA.
DR Proteomes; UP000232157; 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; IPR022398; Peptidase_S8_His-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; PS00137; SUBTILASE_HIS; 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:UP000232157};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 297..562
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 900..972
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 306
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 338
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 515
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1338 AA; 139267 MW; C4B0149FD1304974 CRC64;
MWRVSATPSL EDAPAGELGS ERHAESAGRS VGPPRHQLPR SAHQLNVKGQ PMQKARPRRG
RTALVSGIAV TVALSLTSQL GTATAATPQA PLDLSSRPTL QKQAATTAAV TLITGDTVSL
TTEPDGRQAV SVISGAGTSK TFETVSGQNG DLYVYPDDTT AAVASGTVDR ELFNVSRMVR
DGYGDAKTDE VPAIVDFQGK PTAAALTQKT EGLPGSDNER VMPRLGLSAV HVDKHSAKGF
WQAVKPVHAR SRGAQAATVP GTAGVSKLWY DGKAKVALDK SVPQIGAPEA WAKGYDGKGV
KVAVLDTGAD LNNADVKSEI VQSQSFVNGQ TVQDGHGHGT HVASTIAGSG ANSDGKYKGV
APGADLLIGK VLANSGQGLD SGILAGMDWA VGQGADVVSM SLGGTDTPGE DVLTNAVNSL
SASSGTLFVI AAGNDGRKGE STIGTPGAAD AALTVGAVDK SDALADFSSR GPRLGDMAIK
PEITAPGVDI VAARAAGTTM GTPVDANYTS ANGTSMATPH VAGSAAILKQ RHPGWTGQRI
KDALTAHAKS AADQTVYQQG YGRVDIPAAL DPSLELSGTA DFRVIPWQKG TYPTRSRTLT
LHNNAATDTV MTVTAGAKDA SGTAVPAGTL SLSGAGLSDG RVTVPAGGTA EVTVTLDNNG
LKTGQYGGSV TATSDNGESV HAALGFVTSV EQHDVTLKVT DRFGKTPSAL RFTLHGLDNT
VWQSQTMYAN GTATLSVPLG KYSIEGSLYS ADPAGGAVSY AADLFTVPNI EVSDRDQTFT
VDGTTATDLS VKIKGEKRPL ENGQVTTFIV RDPGTAGGYS SFAGIGNLLN LTDIRQGAIP
SDGATSGALR LETALARREP LVQLEVTGPG HVTIPLKSSV NAKRFEGTKH TELIDLGAGT
EQDFAAADVK GKTVLVSVAD VTKADDQATR AAAGGAVAMI VAPADPGPSG SGVPAGQAIP
VAHATYDNAA TLKGLLAKDK VRIALKGVLE SGYSYNPHFT DDRVPADLAK TVDVKEFAKV
TNTFHSDGAR RLGAENMNIW GPLQVSTGSV GQPLYQGTTR DDYFLAGTGV TYQPSVSANF
NDSTWRMNGQ RASYLTPGKA YTRSWFDAPM RLSQYEFGPC VFCRADVWQN LPGSNGADND
PTHTLSGLTG TWSFYLNGKP ITGFGQLAQE KADYRYVLDQ KLTTDVPGVT LGRHMRTEWD
FSQAAPTTMA IKDCDTAFIP TPKVCESMPV ILLDYDLPLN VLNQARAGLP YTFTVDAGRP
KGWTGSTAMA GAKVSVSYDD GATWKEAKVL RKDSNSFQAL LRHPKLADTN GYVTLKTEAW
DAGGSRTTQT ITRAYALK
//
