ID   C5AP_STRP8              Reviewed;        1150 AA.
AC   Q8NZ80;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=C5a peptidase;
DE            EC=3.4.21.110;
DE   AltName: Full=SCP;
DE   Flags: Precursor;
GN   Name=scpA; OrderedLocusNames=spyM18_2074;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; AE009949; AAL98545.1; -; Genomic_DNA.
DR   RefSeq; WP_011018276.1; NC_003485.1.
DR   AlphaFoldDB; Q8NZ80; -.
DR   SMR; Q8NZ80; -.
DR   MEROPS; S08.020; -.
DR   KEGG; spm:spyM18_2074; -.
DR   HOGENOM; CLU_001768_3_0_9; -.
DR   OMA; MHGMHVA; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034216; C5a_Peptidase.
DR   InterPro; IPR010435; Fn3_5.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
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; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   Pfam; PF06280; fn3_5; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Cell wall; Hydrolase; Peptidoglycan-anchor; Protease; Repeat; Secreted;
KW   Serine protease; Signal; Virulence.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..1113
FT                   /note="C5a peptidase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027159"
FT   PROPEP          1114..1150
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000027160"
FT   DOMAIN          99..581
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REPEAT          1034..1050
FT                   /note="1"
FT   REPEAT          1051..1067
FT                   /note="2"
FT   REPEAT          1068..1084
FT                   /note="3"
FT   REGION          33..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1084
FT                   /note="3 X 17 AA tandem repeats"
FT   MOTIF           1110..1114
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        1031..1073
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1074..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        512
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   MOD_RES         1113
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1150 AA;  126434 MW;  E7E8B8253F4CE326 CRC64;
     MRKKQKLPFD KLAIALMSTS ILLNAQSDIK ANTVTEDTPA AEQAVETPQP TAVSEEVPSS
     KETKTPQTPD NAEETVADKA NDLALQAPAK TADTPATSKA TIRDLNDPSQ VKTLQEKAGK
     GAGTVVAVID AGFDKNHEAW RLTDKTKARY QSKEDLEKAK KEHGITYGEW VNDKVAYYHD
     YSKDGKTAVD QEHGTHVSGI LSGNAPSETK EPYRLEGAMP EAQLLLMRVE IVNGLADYAR
     NYAQAIRDAV NLGAKVINMS FGNAALAYAN LPDETKKAFD YAKSKGVSIV TSAGNDSSFG
     GKTRLPLADH PDYGVVGTPA AADSTLTVAS YSPDKQLTET ATVKTADQQD KEMPVLSTNR
     FEPNKAYDYA YANRGMKEDD FKDVKGKIAL IERGDIDFKD KIANAKKAGA VGVLIYDNQD
     KGFPIELPNV DQMPAAFISR KDGLLLKENP QKTITFNATP KVLPTASGTK LSRFSSWGLT
     ADGNIKPDIA APGQDILSSV ANNKYAKLSG TSMSAPLVAG IMGLLQKQYE IQYPDMTPSE
     RLDLAKKVLM SSATALYDED EKAYFSPRQQ GAGAVDAKKA SAATMYVTDK DNTSSKVHLN
     NVSDKFEVTV TVHNKSDKPQ ELYYQATVQT DKVDGKHFAL APKALYETSW QKITIPANSS
     KQVTVPIDAS RFSKDLLAQM KNGYFLEGFV RFKQDPKKEE LMSIPYIGFR GDFGNLSALE
     KPIYDSKDGS SYYHEANSDA KDQLDGDGLQ FYALKNNFTA LTTESNPWTI IKAVKEGVEN
     IEDIESSEIT ETIFAGTFAK QDDDSHYYIH RHANGKPYAA ISPNGDGNRD YVQFQGTFLR
     NAKNLVAEVL DKEGNVVWTS EVTEQVVKNY NNDLASTLGS TRFEKTRWDG KDKDGKVVAN
     GTYTYRVRYT PISSGAKEQH TDFDVIVDNT TLEVATSATF STEDRRLTLA SKPKTSQPIY
     RERIAYTYMD EDLPTTEYIS PNEDGTFTLP EEAETMEGAT VPLKMSDFTY VVEDMAGNIT
     YTPVTKLLEG HSNKPEQDGS DQAPDKKPEA KPEQDGSGQT PDKKPETKPE KDSSGQTPGK
     TPQKGQPSRT LEKRSSKRAL ATKASARDQL PTTNDKDTNR LHLLKLVMTT FFFGLVAHIF
     KTKRQKETKK