C5AP_STRP6
ID C5AP_STRP6 Reviewed; 1184 AA.
AC Q5X9R0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=C5a peptidase;
DE EC=3.4.21.110;
DE AltName: Full=SCP;
DE Flags: Precursor;
GN Name=scpA; OrderedLocusNames=M6_Spy1718;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
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; CP000003; AAT87853.1; -; Genomic_DNA.
DR RefSeq; WP_011185014.1; NC_006086.1.
DR AlphaFoldDB; Q5X9R0; -.
DR SMR; Q5X9R0; -.
DR MEROPS; S08.020; -.
DR EnsemblBacteria; AAT87853; AAT87853; M6_Spy1718.
DR KEGG; spa:M6_Spy1718; -.
DR HOGENOM; CLU_001768_3_0_9; -.
DR OMA; MHGMHVA; -.
DR Proteomes; UP000001167; Chromosome.
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..1147
FT /note="C5a peptidase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027157"
FT PROPEP 1148..1184
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000027158"
FT DOMAIN 99..581
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REPEAT 1034..1067
FT /note="1"
FT REPEAT 1068..1084
FT /note="2"
FT REPEAT 1085..1101
FT /note="3"
FT REPEAT 1102..1118
FT /note="4"
FT REGION 33..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1118
FT /note="4 X 17 AA tandem repeats"
FT MOTIF 1144..1148
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 33..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1123
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 1147
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1184 AA; 130017 MW; 6FDFB7BF60B0CE01 CRC64;
MRKKQKLPFD KLAIALMSTS ILLNAQSDIK ANTVTEDTPA TEQAVETPQP TAVSEEAPSS
KETKTPQTPD DAEETVADKA NDLAPQAPAK TTDTPATSKA TIRDLNDPSQ VKTLQEKAGK
GAGTVVAVID AGFDKNHEAW RLTDKTKARY QSKEDLEKAK KEHGITYGEW VNDKIAYYHD
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 TQYPDMTPSE
RLDLAKKVLM SSATALYDED EKAYFSPRQQ GAGAVDAKKA SAATMYVTDK DNTSSKVHLN
NVSDTFEVTV TVHNKSDKPQ ELYYQATVQT DKVDGKHFAL APKALYETSW QKITIPANSS
KQVTVPIDAS RFSKDLLAQM KNGYFLEGFV RFKQDLTKEE LMSIPYIGFR GDFGNLSALE
KPIYDSKDGS SYYHEANSDA KDQLDGDGLQ FYALKNNFTA LTTESNPWMI IKAVKEGVEN
IEDIESSEIT ETIFAGTFAK QDDDSHYYIH RHANGKPYAA ISPNGDGNRD YVQFQGTFLR
NAKNLVAEVL DKEGNVVWTS EVTEQVVKNY NNDLASTLGS TRFEKTRWDG KDKDGKVVAN
GTYTYRVRYT PISSGAKEQH TDFDVIVDNT TPEVATSATF STEDRRLTLA SKPKTSQPVY
RERIAYTYMD EDLPTTEYIS PNEDGTFTLP EEAETMEGGT VPLKMSDFTY VVEDMAGNIT
YTPVTKLLEG HSNKPEQDGS DQVPDKKPET KPEQDGSGQA PDKKPETKPE QDGSGQAPDK
KPEAKPEQDG SGQTPDKKPE TKPEKDSSGQ TPGKTPQKGQ PSRTLEKRSS KRALATKASA
RDQLPTTNDK DTNRLHLLKL VMTTFFFGLV AHIFKTKRQK ETKK
