SSPA_STAAR
ID SSPA_STAAR Reviewed; 357 AA.
AC Q6GI34;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SAR1022;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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; BX571856; CAG40026.1; -; Genomic_DNA.
DR RefSeq; WP_000676561.1; NC_002952.2.
DR AlphaFoldDB; Q6GI34; -.
DR SMR; Q6GI34; -.
DR MEROPS; S01.269; -.
DR KEGG; sar:SAR1022; -.
DR HOGENOM; CLU_073589_1_0_9; -.
DR OMA; NFANDDQ; -.
DR OrthoDB; 1468733at2; -.
DR PRO; PR:Q6GI34; -.
DR Proteomes; UP000000596; Chromosome.
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_0000026890"
FT CHAIN 69..357
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000026891"
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 REPEAT 322..324
FT /note="12"
FT REPEAT 325..327
FT /note="13"
FT REPEAT 328..330
FT /note="14"
FT REPEAT 331..333
FT /note="15"
FT REPEAT 337..339
FT /note="16"
FT REPEAT 340..342
FT /note="17"
FT REPEAT 343..345
FT /note="18"
FT REGION 33..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..345
FT /note="18 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..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
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 357 AA; 38639 MW; 0AB1A85D162A0395 CRC64;
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQTDKQQTP KIQKGGNLKP
LEQRERANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHI
VDATHGDPHA LKAFASAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
VFNEKNEVIG IHWGGVPNQF NGAVFINENV RNFLKQNIED INFANDDHPN NPDNPDNPNN
PDNPNNPDNP NNPDNPDNPN NPDNPNNPDN PNNPDQPNNP NNPDNGDNNN SDNPDAA
