ID Q48V13_STRPM Unreviewed; 1645 AA.
AC Q48V13;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
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=prtS {ECO:0000313|EMBL:AAX71443.1};
GN OrderedLocusNames=M28_Spy0329 {ECO:0000313|EMBL:AAX71443.1};
OS Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=319701 {ECO:0000313|EMBL:AAX71443.1, ECO:0000313|Proteomes:UP000009292};
RN [1] {ECO:0000313|EMBL:AAX71443.1, ECO:0000313|Proteomes:UP000009292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS6180 {ECO:0000313|EMBL:AAX71443.1,
RC ECO:0000313|Proteomes:UP000009292};
RX PubMed=16088825; DOI=10.1086/430618;
RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA LeFebvre R.B., Musser J.M.;
RT "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT potential new insights into puerperal sepsis and bacterial disease
RT specificity.";
RL J. Infect. Dis. 192:760-770(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 {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; CP000056; AAX71443.1; -; Genomic_DNA.
DR RefSeq; WP_011284539.1; NC_007296.2.
DR MEROPS; S08.027; -.
DR KEGG; spb:M28_Spy0329; -.
DR HOGENOM; CLU_242589_0_0_9; -.
DR Proteomes; UP000009292; Chromosome.
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; 1.
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; 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; 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; 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};
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}.
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_5038367631"
FT DOMAIN 2..26
FT /note="YSIRK Gram-positive signal peptide"
FT /evidence="ECO:0000259|Pfam:PF04650"
FT DOMAIN 142..676
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 472..545
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 699..812
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT REGION 48..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1605
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; 180916 MW; F02478CAEDD84C51 CRC64;
MEKKQRFSLR KYKSGTFSVL IGSVFLMMTT TVAADELTTT SEPTITNHAQ QQAQHLTNTE
LSSAESQSPD TSQITPKINR EKEQPQGLVS EPTTTELADT DAAPMANTGP DATQKSASLP
PVNTDVHDWV KTKGAWDKGY KGQGKVVAVI DTGIDPAHQS MRISDVSTAK VKSKEDMLAR
QKAAGINYGS WINDKVVFAH NYVENSDNIK ENQFEDFDED WENFEFDAEP KAIKKHKIYR
PQSTQAPKET VIKTEETDGS HDIDWTQTDD DTKYESHGMH VTGIVAGNSK EAAATGERFL
GIAPETQVMF MRVFANDVMG SAESLFIKAI EDAVALGADV INLSLGTANG AQLSGSKPLM
EAIEKAKKAG VSVVVAAGNE RVYGSDHDDP LATNPDYGLV GSPSTGRTPT SVAAINSKWV
IQRLMTVKEL ENRADLNHGK AIYSESVDFK DIKDSLGYDK SHQFAYVKES TDAGYNAQDV
KGKIALIERD PNKTYDEMIA LAKKHGALGV LIFNNKPGQS NRSMRLTANG MGIPSAFISH
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 KYVSVEDNKT
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 EGNTKVNTLP
NEVHELSLRL VKVGDASDST GDHKVMSKNN SQALTASATP TKTTTSATAK ALPSAGEKMG
LKLRIVGLVL LGLTCVFSRK KSTKD
//
