SSPA_STAAS
ID SSPA_STAAS Reviewed; 333 AA.
AC Q6GAG4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutamyl endopeptidase;
DE EC=3.4.21.19;
DE AltName: Full=Endoproteinase Glu-C;
DE AltName: Full=Staphylococcal serine proteinase;
DE AltName: Full=V8 protease;
DE AltName: Full=V8 proteinase;
DE Flags: Precursor;
GN Name=sspA; OrderedLocusNames=SAS0984;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal
CC side of aspartate and glutamate. Along with other extracellular
CC proteases it is involved in colonization and infection of human
CC tissues. Required for proteolytic maturation of thiol protease SspB and
CC inactivation of SspC, an inhibitor of SspB. It is the most important
CC protease for degradation of fibronectin-binding protein (FnBP) and
CC surface protein A, which are involved in adherence to host cells. May
CC also protect bacteria against host defense mechanism by cleaving the
CC immunoglobulin classes IgG, IgA and IgM. May be involved in the
CC stability of secreted lipases (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.; EC=3.4.21.19;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10083};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads
CC to the activation of SspA (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The cascade of activation of extracellular proteases
CC proceeds from the metalloprotease aureolysin (aur), through SspA to
CC SspB. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR EMBL; BX571857; CAG42759.1; -; Genomic_DNA.
DR RefSeq; WP_000676532.1; NC_002953.3.
DR AlphaFoldDB; Q6GAG4; -.
DR SMR; Q6GAG4; -.
DR MEROPS; S01.269; -.
DR KEGG; sas:SAS0984; -.
DR HOGENOM; CLU_073589_1_0_9; -.
DR OMA; NFANDDQ; -.
DR PRO; PR:Q6GAG4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR008353; Peptidase_S1B_tx.
DR InterPro; IPR028301; V8_his_AS.
DR InterPro; IPR000126; V8_ser_AS.
DR PRINTS; PR01774; EXFOLTOXIN.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00672; V8_HIS; 1.
DR PROSITE; PS00673; V8_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Repeat; Secreted; Serine protease; Signal; Virulence;
KW Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..68
FT /evidence="ECO:0000250"
FT /id="PRO_0000026892"
FT CHAIN 69..333
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000026893"
FT REPEAT 289..291
FT /note="1"
FT REPEAT 292..294
FT /note="2"
FT REPEAT 295..297
FT /note="3"
FT REPEAT 298..300
FT /note="4"
FT REPEAT 301..303
FT /note="5"
FT REPEAT 304..306
FT /note="6"
FT REPEAT 307..309
FT /note="7"
FT REPEAT 310..312
FT /note="8"
FT REPEAT 313..315
FT /note="9"
FT REPEAT 316..318
FT /note="10"
FT REPEAT 319..321
FT /note="11"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..321
FT /note="11 X 3 AA repeats of P-[DN]-N"
FT COMPBIAS 33..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT SITE 68..69
FT /note="Cleavage; by aureolysin"
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 35970 MW; 5FABB3E6098544C4 CRC64;
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QSQSSKQQTP KIQKGGNLKP
LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV
VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN
PDNPNNPDNP NNPNNPDNPD NGDNNNSDNP DAA
