ID A0A0M2HDR9_9MICO Unreviewed; 1284 AA.
AC A0A0M2HDR9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=apr_2 {ECO:0000313|EMBL:KJL44719.1};
GN ORFNames=RS82_00677 {ECO:0000313|EMBL:KJL44719.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL44719.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL44719.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL44719.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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}.
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:KJL44719.1}.
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DR EMBL; JYJA01000024; KJL44719.1; -; Genomic_DNA.
DR RefSeq; WP_052676672.1; NZ_JYJA01000024.1.
DR PATRIC; fig|69370.6.peg.701; -.
DR Proteomes; UP000034098; 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:UP000034098};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 235..487
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 811..895
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 450
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1284 AA; 133736 MW; 4A3AC7B818A34FFE CRC64;
MSRPQPFGPR LRPIVAATSG LTIAIAGIGL TTLPAAATSA PDNSPATRAV AGSSHSVTLI
TGDRVTVTDL SDGTHTVSID TAVDGAGVRT YEAAGDLHVV PDAALPYLAS GALDSDLFNV
TLLIDYGYDD ATVDATPIIV EQDTAAARSF TAPVPGFDVL TPLESIGGAA ATLGHDAAAS
AWQSLTAPTA RSFSTAPGFA GGIQSIHLDG KVRATLDSSV PYIDAPEAWA EGYTGQGVTV
AVLDTGYDDT HLDLQGHVSA ESKSFVPGED VDSDPNGHGT HVASTIAGTG AASGGTHRGV
ADGAQLLVGK VLGADGYGQD SWIIDAMEWA GQNAPIVSMS LGSTEASDGK DLMAESLNRI
SEETGTLFVV AAGNAGAPET IGAPGSAERA LTVGSVDDPS GSLSYFTSQG PLARSGAMKP
DVTGPGNDVT AARSADSPGE GSYVAMSGTS MATPHVAGAA AILLGAHPDY TSAQLKAALA
SSAVDLGYTP YQGGTGVINV AAALDAPVIA SGTGDFGMLA WGQAPAPVTR TIEYTNRTDA
ELTVALEPTL SDTTPDDGTG EPGPLSDGIA FDALTIDSAS LTIPAGETRS VTMTVDPAKV
PAGTQLSGAL VGLVDGDAVT RTALGTIAEA ERYDLTITAT GFDGNPVQTY AFLWNAATQF
AEPIPVDGET TLRLMKGDYS VVSFMELSRT PDTIASVLVG EPTLQLDGDK TVALDARAAK
QVTLDVGEKG LEPVFRRMDM KVGDFLASAT MPVWTDEMWA QPMKIDDADF GFTTRWRLQT
PLLTVSAGKN ALDLILQPGS TFLDGSFKAT AVEAGSGRPD ELAAAEVGGK IAVVTRSTDL
SPSEQAANAA AAGAKLLVLV NDADGEFSTW VGSEADFSNV SIPVAGISGV EGRALLGQLG
GRKKVTLSAV GVPTTDVVYD IAEYGDGQIP QKLAYKHSSR DLARIDTRFH GQQEELAEFR
YDFVPGAQYG SGFPFRAQRG MDRTEWVNTD SLRWNQWVAV SSVMWEIRDK QTTYTRGERT
SEEYFGGIVR PYVATGFWVP YRVSDWAQVN IPSWADGGDA DHTGTFDTWV EPSTVHQTAD
VYIDGQLVKQ QEHQGVNLFD LPDGDQQWRV VSTATHDGAH LEGSTRTVSD WTFRSAGKLG
DWGNRLLPMI QAYYDVDVNI DNQVGQGRKK GSGVTLGLEL GHVAGTSPAG AITGATLEAR
GENGQWRPVE LKSAKTDAPT GAVEGDGDIF VTSRAWVSGF TAQIPVPDKG GWVDLRVTAK
DAEGNTFTQE IEKAFEATPA KGVR
//
