C5AP_STRPY
ID C5AP_STRPY Reviewed; 1167 AA.
AC P15926;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=C5a peptidase;
DE EC=3.4.21.110;
DE AltName: Full=SCP;
DE Flags: Precursor;
GN Name=scpA;
OS Streptococcus pyogenes.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 32-41.
RX PubMed=2406246; DOI=10.1016/s0021-9258(19)39748-0;
RA Chen C.C., Cleary P.P.;
RT "Complete nucleotide sequence of the streptococcal C5a peptidase gene of
RT Streptococcus pyogenes.";
RL J. Biol. Chem. 265:3161-3167(1990).
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; J05229; AAA26960.1; -; Genomic_DNA.
DR PIR; A35066; A35066.
DR RefSeq; WP_002991221.1; NZ_WXZG01000024.1.
DR PDB; 1XF1; X-ray; 1.90 A; A/B=106-1031.
DR PDB; 3EIF; X-ray; 1.90 A; A=97-1032.
DR PDBsum; 1XF1; -.
DR PDBsum; 3EIF; -.
DR AlphaFoldDB; P15926; -.
DR SMR; P15926; -.
DR MEROPS; S08.020; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR OMA; MHGMHVA; -.
DR SABIO-RK; P15926; -.
DR EvolutionaryTrace; P15926; -.
DR PHI-base; PHI:7312; -.
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; Direct protein sequencing; Hydrolase;
KW Peptidoglycan-anchor; Protease; Repeat; Secreted; Serine protease; Signal;
KW Virulence.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:2406246"
FT CHAIN 32..1130
FT /note="C5a peptidase"
FT /id="PRO_0000027151"
FT PROPEP 1131..1167
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000027152"
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 REGION 34..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1101
FT /note="4 X 17 AA tandem repeats"
FT MOTIF 1127..1131
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 34..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1106
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 1130
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:1XF1"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1XF1"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1XF1"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 235..251
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1XF1"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 334..344
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:1XF1"
FT TURN 378..383
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 398..407
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 440..448
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 514..531
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 537..552
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 577..582
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 584..593
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 604..614
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 620..634
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 637..647
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 659..668
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 673..679
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 684..695
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 702..711
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 758..765
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 768..776
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 791..794
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 819..821
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 824..829
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 832..836
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 842..850
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:1XF1"
FT TURN 874..876
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 879..882
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 900..913
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 919..927
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:1XF1"
FT TURN 942..944
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 946..949
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 959..972
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 974..979
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 991..994
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 1009..1014
FT /evidence="ECO:0007829|PDB:1XF1"
FT STRAND 1019..1023
FT /evidence="ECO:0007829|PDB:1XF1"
FT HELIX 1024..1028
FT /evidence="ECO:0007829|PDB:1XF1"
SQ SEQUENCE 1167 AA; 128264 MW; D2DDC52E5752DA5D CRC64;
MRKKQKLPFD KLAIALMSTS ILLNAQSDIK ANTVTEDTPV TEQAVETPQP TAVSEEVPSS
KETKTPQTPD DAEETIADDA NDLAPQAPAK 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 AMVKTDDQQD KEMPVLSTNR
FEPNKAYDYA YANRGMKEDD FKDVKGKIAL IERGDIDFKD KVANAKKAGA VGVLIYDNQD
KGFPIELPNV DQMPAAFISR KDGLLLKDNP QKTITFNATP KVLPTASGTK LSRFSSWGLT
ADGNIKPDIA APGQDILSSV ANNKYAKLSG TSMSAPLVAG IMGLLQKQYE TQYPDMTPSE
RLDLAKKVLM SSATALYDED EKAYFSPRQQ GAGAVDAKKA SAATMYVTDK DNTSSKVHLN
NVSDKFEVTV TVHNKSDKPQ ELYYQATVQT DKVDGKHFAL APKVLYEASW QKITIPANSS
KQVTVPIDAS RFSKDLLAQM KNGYFLEGFV RFKQDPTKEE LMSIPYIGFR GDFGNLSAVE
KPIYDSKDGS SYYHEANSDA KDQLDGDGLQ FYALKNNFTA LTTESNPWTI IKAVKEGVEN
IEDIESSEIT ETIFAGTFAK QDDDSHYYIH RHANGEPYAA ISPNGDGNRD YVQFQGTFLR
NAKNLVAEVL DKEGNVVWTS EVTEQVVKNY NNDLASTLGS TRFEKTRWDG KDKDGKVVAN
GTYTYRVRYT PISSGAKEQH TDFDVIVDNT TPEVATSATF STEDRRLTLA SKPKTSQPVY
RERIAYTYMD EDLPTTEYIS PNEDGTFTLP EEAETMEGAT VPLKMSDFTY VVEDMAGNIT
YTPVTKLLEG HSNKPEQDGS GQTPDKKPEA KPEQDGSDQA PDKKPEAKPE QDGSGQTPDK
KPETKPEKDS SGQTPGKTPQ KGQPSRTLEK RSSKRALATK ASTRDQLPTT NDKDTNRLHL
LKLVMTTFFF GLVAHIFKTK RQKETKK
