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Database: UniProt
Entry: A0A0C2RMP5_9BACL
LinkDB: A0A0C2RMP5_9BACL
Original site: A0A0C2RMP5_9BACL 
ID   A0A0C2RMP5_9BACL        Unreviewed;      1543 AA.
AC   A0A0C2RMP5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=KR50_34170 {ECO:0000313|EMBL:KIL43014.1};
OS   Jeotgalibacillus campisalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX   NCBI_TaxID=220754 {ECO:0000313|EMBL:KIL43014.1, ECO:0000313|Proteomes:UP000031972};
RN   [1] {ECO:0000313|EMBL:KIL43014.1, ECO:0000313|Proteomes:UP000031972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF-57 {ECO:0000313|EMBL:KIL43014.1,
RC   ECO:0000313|Proteomes:UP000031972};
RA   Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT   "Jeotgalibacillus campisalis genome sequencing.";
RL   Submitted (JAN-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.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-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:KIL43014.1}.
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DR   EMBL; JXRR01000022; KIL43014.1; -; Genomic_DNA.
DR   RefSeq; WP_041061215.1; NZ_JXRR01000022.1.
DR   PATRIC; fig|220754.4.peg.3432; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000031972; 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; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR   Gene3D; 3.40.50.12090; -; 2.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR007253; Cell_wall-bd_2.
DR   InterPro; IPR010435; Fn3_5.
DR   InterPro; IPR013783; Ig-like_fold.
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; PF04122; CW_binding_2; 3.
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; PS00137; SUBTILASE_HIS; 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:UP000031972};
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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1543
FT                   /note="C5a peptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002154498"
FT   DOMAIN          201..663
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          459..532
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          687..813
FT                   /note="Fn3-like"
FT                   /evidence="ECO:0000259|Pfam:PF06280"
FT   ACT_SITE        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        276
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        601
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1543 AA;  165703 MW;  B2916D5476BA8784 CRC64;
     MTKKWKNNVT AALALSLVLG NSSVALGQDN QNDAPKKDAN GEVPVNVLSN AQAKMAKLDQ
     KAKVTADKAA LKESDMVRVI VEVAGETAIE HATKKGVLYK ELSDSEKENF EQEAASSQQS
     VKQSISSKGV DIEYKNSFSA SVNGFSGIIQ YKDFGAIESL PGVKKVYIAN EYERPEFEED
     MVTSHEFIQS YQTWADAKYK GEGMIVSVID SGTDVDHRDF VLSDGVEGEL TKEEVSALKD
     ENSVTGNFYN EKVPYAYNYY DLNDTVEDLG PDASMHGMHV AGTVAANGDT ENGGIKGVAP
     EAQILGMKVF SNDPNFASTY SDIYLKAIDD SIKLGADVLN MSLGSTASFY EEESPEDLAI
     TRAVENGIVS TVSAGNSGHI GRGYSNPHYE NPDIGLVGAP GLNADTLQVA ASGNYMDLYT
     HSVNGEGVPE FKGYGIDDWS KLGEVEVVSL KALSGNSGAL GAPADYSGID VKGKVVVVER
     GGLPFVDKTV NAANAGAAGI IVYNSTSPVF YKDQGGWDIP FMKVERAAGL DLEAVLADGS
     SLMMDVTQTA KEEGPEVGRA TDFTSWGVTP DLEFKPEITA PGGGILSTVN DDEYTVMSGT
     SMAAPHVAGG SALVQQYLLD DDRFNEYNSD ERTRLAKALL MNTADIIHDL NGQPFSPRRQ
     GAGMMQTYAA VSTPVFVTDS ETNEAKVNLK DFTSKTVSMT LTATNLTGED AEYNVDTSVL
     ADTFVKDGDS TYNALVAGDL EGAVVSGPES VTVPANGSVD VTVSIDLTNA KVKGIDEDGN
     EELIDLPADQ FVEGFVKLVS TDLENPDLAV PYLGFYGKWE NPDIVDNMSF EGEDRFYNTP
     SSVVQLNREN IPTFSSGIEV DGEIVYPLST KNKDGLYDDI NVAPSFLRNA KEVQFNVLNG
     ENTKLKTISL ENNIRKNYAA AGQYSYSGAR VWNSSVKDKI VDDGMYFYEI KSRVDYDGAK
     WQSKKVPVYV DNTAPEVNDV SFDKDTNTLS FTGVDEGVGI LWYDLYINGQ YVTPTEKLNG
     DTTSVNLSNY GFSAEEIQSL EIVPVDKAGN VGYEASFVDD GDAPIIYLDD NAPIALNYYK
     TRTIPVAGKI VEENALESVK VNGKEVPFTP STDGFVFSTE VTVESDGKHD ITIEATDVNG
     NSTSIARGFW VDTVAPQVVV NTDELVNNST DQVEVDVLLS DNFNGVELSL EDDVLFSSMN
     TTSDETKPFE GTVPVTLDLE EGSNTFEFKA IDTAGNETVY ELSITRNDSG LFVERISGKN
     RYETAVELSQ TEWDSADTVI LARGDNYADA LAGVPLTSMH DGPLLLSRTA ALPSSTLDEI
     KRLGAKKVVV LGGEGAVSAD VVKTLKNQGI TVERISGKDR YETAAKIAEK FGKSSNAVVV
     NGQNFPDALS AASYAAQQKM PILLTKSSSL PKATKDALAK LEANRTFVVG GSGVVSNEVM
     GQVPNAHRIS GKDRYATSLE VAKFFGQDSD TVYVATGRDF ADALSGSAVA AKSGSGLYLV
     GSSVSDDLGQ HLQDEDFNYA KVIGGKTIVS EDIVQQLNDF LEE
//
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