ID A0A0M8MIB6_9MICO Unreviewed; 1036 AA.
AC A0A0M8MIB6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=XI38_01530 {ECO:0000313|EMBL:KOS12108.1};
OS Microbacterium chocolatum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS12108.1, ECO:0000313|Proteomes:UP000037737};
RN [1] {ECO:0000313|EMBL:KOS12108.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIT 101 {ECO:0000313|EMBL:KOS12108.1};
RA Li X., Xu Y.;
RT "Complete genome sequence of Microbacterium chocolatum SIT 101, a bacterium
RT enantioselectively hydrolyzing mesomeric diesters.";
RL Submitted (APR-2015) 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:KOS12108.1}.
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DR EMBL; LAVO01000001; KOS12108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8MIB6; -.
DR KEGG; mcw:A8L33_04755; -.
DR PATRIC; fig|84292.3.peg.319; -.
DR Proteomes; UP000037737; 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; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
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 InterPro; IPR034213; S8_Vpr-like.
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:UP000037737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1036
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005818437"
FT DOMAIN 183..620
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 429..516
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 824..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 584
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1036 AA; 105815 MW; B6FC364B423E2BE7 CRC64;
MVIATAVPIL SLGAMPAAWA VEGGPEPVPD GSISDTFETP LPRGVADSLQ RASGQVEVTV
RLDQPAIAEV VADGALAEGD VPAEPVQQET RDVVATQQEG FLAEAANLGA SEIGRTQLAA
NVVVVSVDAA QLETLAAIDG VVSVNPLNRY EKHELPQDTA SGSLSQAIDY VQARPLHDAG
IDGAGVRVAV LDSGIDFTHR NLGGPGTPEV VEECFAGADA DVTGVCAEFF GPDAPKVKGG
YDFVGDVWPN GDVIPDSNPI DSGPEGGHGT HVADIIAGRS ADGAHQGIAP GAELYGVKVC
SAVSTSCNGV AILQGLDWSL DPNGDGDISD AVDIVNLSLG SSYGQDQDDS SFAADNLVRA
GIVVVASAGN SADRPFIVGS PSSAPGVISV AQTALPDDLQ WVLDPSSGDA ISNAVHQAWS
PVPEGVISAP LARPGDEGGV GCSDEAFAGF PEGSIALIQR GVCNVSDKAV FAQAAGAVAV
VIFNNAPGDP PSFSFGSAEP VVVPTFTISQ AAGQALVAAL GAGEVTITID PASAIPLTNT
MVGTSSRGLT VTGLRAKPDI GAPGAWLSAE TQTGTEVTNF GGTSGAAPVV SGVAALVLQK
RPDATPAEVK ARLLNGADST NRTPTADGFI ATPISRVGAG EVRALPAADA VGVLATAGTG
GNVGLGIPSV TRSERFTVDL TLTNTTDERK RYDMAAAFRD ETDAASRAVD LQISPRNVTV
AAGQSKKVSV RVTIDGSRLQ DWPFDSAGAI GDGSALNGPE FDGWITATAG DEELHVGWTV
LPRKAAEVTA PKSVKLDRRG EADLTLKNDS RVGTGGVEMF ALTGTSERQP KPAAGDPGTP
GSNAARIDLA ATGVRTVDDV VQFAVATYDR RTVLTYPAEF DVYVDVDEDG TDDYVVYNAE
AGGFGLTGQS VVYVYDLATD AASAFYYTDG GFDSSTQILT APLAALGLEA GQTFSYTVLA
IDNYFTGAVT DSIEGQRFTV GGEKYLVPTT TEVGPRDRVT LDVTANPAAG ESTQTGLLLL
NRSAAKDDFS LVEVRG
//
