C5AP_STRP1
ID C5AP_STRP1 Reviewed; 1181 AA.
AC P58099; Q48WE2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=C5a peptidase;
DE EC=3.4.21.110;
DE AltName: Full=SCP;
DE Flags: Precursor;
GN Name=scpA; OrderedLocusNames=SPy_2010, M5005_Spy1715;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AE004092; AAK34691.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52333.1; -; Genomic_DNA.
DR RefSeq; NP_269970.1; NC_002737.2.
DR PDB; 7BJ3; X-ray; 2.60 A; A=32-1032.
DR PDBsum; 7BJ3; -.
DR AlphaFoldDB; P58099; -.
DR SMR; P58099; -.
DR STRING; 1314.HKU360_01830; -.
DR MEROPS; S08.020; -.
DR PaxDb; P58099; -.
DR EnsemblBacteria; AAK34691; AAK34691; SPy_2010.
DR KEGG; spy:SPy_2010; -.
DR KEGG; spz:M5005_Spy1715; -.
DR PATRIC; fig|160490.10.peg.1748; -.
DR HOGENOM; CLU_001768_3_0_9; -.
DR OMA; MHGMHVA; -.
DR BRENDA; 3.4.21.110; 11745.
DR Proteomes; UP000000750; 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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Hydrolase; Peptidoglycan-anchor; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Virulence.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..1147
FT /note="C5a peptidase"
FT /id="PRO_0000027153"
FT PROPEP 1148..1181
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000027154"
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 REPEAT 1085..1101
FT /note="4"
FT REPEAT 1102..1118
FT /note="5"
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="5 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 91..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"
FT CONFLICT 1072..1088
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:7BJ3"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 235..251
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:7BJ3"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 334..344
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 398..408
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 440..447
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:7BJ3"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 511..532
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 538..552
FT /evidence="ECO:0007829|PDB:7BJ3"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 577..582
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 595..602
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 604..614
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 620..634
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 637..647
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 659..668
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 673..679
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 684..695
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 700..711
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 758..765
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 768..776
FT /evidence="ECO:0007829|PDB:7BJ3"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 791..794
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:7BJ3"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 819..821
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 824..829
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 832..836
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 842..850
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 852..854
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 900..913
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 919..927
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 938..941
FT /evidence="ECO:0007829|PDB:7BJ3"
FT TURN 942..945
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 946..951
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 959..979
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 991..994
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 1008..1014
FT /evidence="ECO:0007829|PDB:7BJ3"
FT STRAND 1019..1023
FT /evidence="ECO:0007829|PDB:7BJ3"
FT HELIX 1024..1028
FT /evidence="ECO:0007829|PDB:7BJ3"
SQ SEQUENCE 1181 AA; 129487 MW; 3F9FC51763419CFC CRC64;
MRKKQKLPFD KLAIALMSTS ILLNAQSDIK ANTVTEDTPA TEQAVETPQP TAVSEEAPSS
KETKTPQTPD DAEETIADDA NDLAPQAPAK TADTPATSKA TIRDLNDPSQ VKTLQEKAGK
GAGTVVAVID AGFDKNHEAW RLTDKTKARY QSKEDLEKAK KEHGITYGEW VNDKVAYYHD
YSKDGKTAVD QEHGTHVSGI LSGNAPSETK EPYRLEGAMP EAQLLLMRVE IVNGLADYAR
NYAQAIIDAV 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
NVSDKFEVTV TVHNKSDKPQ ELYYQATVQT DKVDGKLFAL APKALYETSW QKITIPANSS
KQVTIPIDVS QFSKDLLAPM KNGYFLEGFV RFKQDPTKEE LMSIPYIGFR GDFGNLSALE
KPIYDSKDGS SYYHEANSDA KDQLDGDGLQ FYALKNNFTA LTTESNPWTI IKAVKEGVEN
IEDIESSEIT ETIFAGTFAK QDDDSHYYIH RHANGKPYAA ISPNGDGNRD YVQFQGTFLR
NAKNLVAEVL DKEGNVVWTS EVTEQVVKNY NNDLASTLGS TRFEKTRWDG KDKDGKVVAN
GTYTYRVRYT PISSGAKEQH TDFDVIVDNT TPEVATSATF STEDRRLTLA SKPKTSQPVY
RERIAYTYMD EDLPTTEYIS PNEDGTFTLP EEAETMEGAT VPLKMSDFTY VVEDMAGNIT
YTPVTKLLEG HSNKPEQDGS DQAPDKKPET KPEQDGSGQA PDKKPETKPE QDGSGQTPDK
KPETKPEQDG SGQTPDKKPE TKPEKDSSGQ TPGKTPQKGQ PSRTLEKRSS KRALATKAST
KDQLPTTNDK DTNRLHLLKL VMTTFFLGLV AHIFKTKRTE D
