ID Q202A4_STRPY Unreviewed; 1645 AA.
AC Q202A4;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=C5a peptidase {ECO:0000256|ARBA:ARBA00020956};
DE EC=3.4.21.110 {ECO:0000256|ARBA:ARBA00012942};
DE AltName: Full=SCP {ECO:0000256|ARBA:ARBA00030432};
GN Name=cepA {ECO:0000313|EMBL:ABD72245.1};
OS Streptococcus pyogenes.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1314 {ECO:0000313|EMBL:ABD72245.1};
RN [1] {ECO:0000313|EMBL:ABD72245.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H343 {ECO:0000313|EMBL:ABD72245.1};
RX PubMed=16088827; DOI=10.1086/432485;
RA Edwards R.J., Taylor G.W., Ferguson M., Murray S., Rendell N., Wrigley A.,
RA Bai Z., Boyle J., Finney S.J., Jones A., Russell H.H., Turner C., Cohen J.,
RA Faulkner L., Sriskandan S.;
RT "Specific C-terminal cleavage and inactivation of interleukin-8 by invasive
RT disease isolates of Streptococcus pyogenes.";
RL J. Infect. Dis. 192:783-790(2005).
RN [2] {ECO:0000313|EMBL:ABD72245.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H343 {ECO:0000313|EMBL:ABD72245.1};
RA Turner C., Jones M.D., Sriskandan S.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABD72245.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H343 {ECO:0000313|EMBL:ABD72245.1};
RX PubMed=19591574; DOI=10.1086/603541;
RA Turner C.E., Kurupati P., Jones M.D., Edwards R.J., Sriskandan S.;
RT "Emerging role of the interleukin-8 cleaving enzyme SpyCEP in clinical
RT Streptococcus pyogenes infection.";
RL J. Infect. Dis. 200:555-563(2009).
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 {ECO:0000256|ARBA:ARBA00002909}.
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; Evidence={ECO:0000256|ARBA:ARBA00001404};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; DQ413038; ABD72245.1; -; Genomic_DNA.
DR RefSeq; WP_020904927.1; NZ_CAAJEO010000008.1.
DR MEROPS; S08.027; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02133; PA_C5a_like; 1.
DR CDD; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR Gene3D; 2.60.40.1710; Subtilisin-like superfamily; 1.
DR InterPro; IPR034216; C5a_Peptidase.
DR InterPro; IPR010435; Fn3_5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR046450; PA_dom_sf.
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 InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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 {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Viral envelope protein {ECO:0000313|EMBL:ABD72245.1};
KW Virion {ECO:0000313|EMBL:ABD72245.1}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1645
FT /note="C5a peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038857039"
FT DOMAIN 1612..1645
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 46..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 615
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1645 AA; 180704 MW; 722A5F201E9B8750 CRC64;
MEKKQRFSLR KYKSGTFSVL IGSVFLMMTT TVAADELTTT SEPTITNHAQ QQAPPLTNTE
LSSAESQPQD TSQVTPETNR EKEQPQGLVS EPTTTELADT DAAPMANTGS DATQKSASLP
PVNTDVHDWV KTKGAWDKGY KGQGKVVAVI DTGIDPAHQS MRISDVSTAK VKSKEDMLAR
QKAAGINYGS WINDKVVFAH NYVENSDNIK ENQFGDFDED WENFEFDAEP KAIKKNKIYR
PQSTQAPKET VIKTEETDGS HDIDWTQTDD ETKYESHGMH VTGIVAGNSK EAAATGERFL
GIAPEAQVMF MRVFANDVMG SAESLFIKAI EDAVALGADV INLSLGTANG AQLSGSKPLI
EAIEKAKKAG VSVVVAAGNE RVYGSDHDDP LATNPDYGLV GSPSTGRTPT SVAAINSKWV
IQRLMTVKEL ENRADLNHGK AIYSESVDFK DIKDSLGYDK SHQFAYVKES TDAGYKAQDV
KGKIALIERD PNKTYDEMIA LAKKHGALGV LIFNNKPGQS NRSMRLTANG MGIPSAFISY
EFGKAMSQLN GNGTGSLEFD SVVSKAPSQK GNEMNHFSNW GLTSDGYLKP DITAPGGDIY
STYNDNHYGS QTGTSMASPQ IAGASLLVKQ YLEKTQPNLP KEKIADIVKN LLMSNAQIHV
NPETKTTTSP RQQGAGLLNI DGAVTSGLYV TGKDNYGSIS LGNITDTMTF DVTVHNLSNK
AKTLRYDTEL LTDHVDPQKG RFTLTSRSLK TYQGGEVTVP ANGKVTVRVT MDVSQFTKEL
TKQMPNGYYL EGFVRFRDSQ DDQLNRVNIP FVGFKGQFEN LAVAEESIYR LKSQGKTGFY
FDESGPKDDI YVGKHFTGLV TLGSETNVST KTISDNGLHT LGTFKNADGK FILEKNAQGN
PVLAISPNGD NNQDFAAFKG VFLRKYQGLK ASVYHASDKE HKNPLWVSPE SFKGDKNFNS
DIRFAKSTTL LGTAFSGKSL TGAELPDGYY HYVVSYYPDV VGAKRQEMTF DMILDRQKPV
LSQATFDPET NRFKPEPLKD RGLAGVRKDS VFYLERKDNK PYTVTINDSY KYVSVADNKT
FVERQADGSF ILPLDKAKLG DFYYMVEDFA GNVAIAKLGD HLPQTLGKTP IKLKLTDGNY
QTKETLKDNL EMTQSDTGLV TNQAQLAVVH RNQPQSQLTK MNQDFFISPN EDGNKDFVAF
KGLKNNVYND LTVNVYAKDD HQKQTPIWSS QAGASASAIE STAWYGITAR GSKVMPGDYQ
YVVTYRDEHG KEHQKQYTIS VNDKKPMITQ GRFDTINGVD HFTPDKTKAL GSSGIVREEV
FYLAKKNGRK FDVTEGKDGI TVSDNKVYIP KNPDGSYTIS KRDGVTLSDY YYLVEDRAGN
VSFATLRDLK AVGKDKAVVN FGLDLPVPED KQIVNFTYLV RDADGKPIEN LEYYNNSGNS
LILPYGKYTV ELLTYDTNAA KLESDKIVSF TLSADNNFQQ VTFKMTMLAT SQITAHFDHL
LPEGSRVSLK TAQGQLIPLE QSLYVPKAYG KTVQEGTYEV VVSLPKGYRI EGNTKVNALP
NEVHELSLRL VKVGDASDST GDHKVMSKNN SQALTASATP TKTTTSATAK ALPSTGEKMG
LKLRIVGLVL LGLTCVFSRK KSTKD
//
