C5AP_STRPQ
ID C5AP_STRPQ Reviewed; 1169 AA.
AC P0DD35; Q79W61; Q8K5Q0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=C5a peptidase;
DE EC=3.4.21.110;
DE AltName: Full=SCP;
DE Flags: Precursor;
GN Name=scpA; OrderedLocusNames=SPs1724;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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; BA000034; BAC64819.1; -; Genomic_DNA.
DR RefSeq; WP_011055051.1; NC_004606.1.
DR AlphaFoldDB; P0DD35; -.
DR SMR; P0DD35; -.
DR MEROPS; S08.020; -.
DR KEGG; sps:SPs1724; -.
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..1132
FT /note="C5a peptidase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000411455"
FT PROPEP 1133..1169
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000411456"
FT DOMAIN 101..583
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REPEAT 1036..1052
FT /note="1"
FT REPEAT 1053..1069
FT /note="2"
FT REPEAT 1070..1086
FT /note="3"
FT REPEAT 1087..1103
FT /note="4"
FT REGION 33..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1103
FT /note="4 X 17 AA tandem repeats"
FT MOTIF 1129..1133
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 33..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 514
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MOD_RES 1132
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1169 AA; 128228 MW; 8648F83AEC4025A5 CRC64;
MRKKQKLPFD KLAIALMSTS ILLNAQSDIK ANTVTEDTPA TEQAVEVPQQ TAVSEEAPSS
SSKETNPPQT PDDAEETVAD KANDLAPQAP AKTADIPATS KETIRDLNDP SHVKTLQEKA
GKGAGTVVAV IDAGFDKNHE AWRLTDKSKA RYQSKEDLEK AKKDHGITYG EWVNDKVAYY
HDYSKDGKTA VDQEHGTHVS GILSGNAPSE TKEPYRLEGA MPEAQLLLMR VEIVNGLADY
ARNYAQAIRD AVNLGAKVIN MSFGNAALAY ANLPDETKKA FDYAKSKGVS IVTSAGNDSS
FGGKTRLPLA DHPDYGVVGT PAAADSTLTV ASYSPDKQLT ETATVKTADQ QDKEMPVLST
NRFEPNKAYD YAYANRGTKE DDFKDVKGKI ALIERGDIDF KDKIANAKKA GAVGVLIYDN
QDKGFPIELP NVDQMPAAFI SRKDGLLLKD NSKKTITFNA TPKVLPTASG TKLSRFSSWG
LTADGNIKPD IAAPGQDILS SVANNKYAKL SGTSMSAPLV AGIMGLLQKQ YETQYPDMTP
SERLDLAKKV LMSSATALYD EDEKAYFSPR QQGAGAVDAK KASAATMYVT DKDNTSSKVH
LNNVSDKFEV TVTVHNKSDK PQELYYQATV QTDKVDGKHF ALAPKALYET SWQKITIPAN
SSKQVTVPID ASRFSKDLLA QMKNGYFLEG FVRFKQDPTK EELMSIPYIG FRGDFGNLSA
LEKPIYDSKD GSSYYHEANS DAKDQLDGDG LQFYALKNNF TALTTESNPW TIIKAVKEGV
ENIEDIESSE ITETIFAGTF AKQDDDSHYY IHRHANGKPY AAISPNGDGN RDYVQFQGTF
LRNAKNLVAE VLDKEGDVVW TSEVTEQVVK NYNNDLASTL GSTRFEKTRW DGKDKDGKVV
ANGTYTYRVR YTPISSGAKE QHTDFDVIVD NTTPEAATSA TFSAEDRRLT LASKPKTSQP
VYRERIAYTY MDEDLPTTEY ISPNEDGTFT LPEEAETMEG ATVPLKMSDF TYVVEDMAGN
ITYTPVTNLL EGHSNKPEQD GSDQVPDKTP ETKPEQDGSG QAPDKKPEAK PEQDGSGQAP
DKKPETKPEK DSSGQTPGKT PQKGQPSRTL EKRSSKRALA TKASARDQLP TTNDKDTNRL
HLLKLVMTTF FFGLVAHIFK TKRQKETKK
