SSPA_STAAC
ID SSPA_STAAC Reviewed; 336 AA.
AC Q5HH35;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SACOL1057;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW36522.1; -; Genomic_DNA.
DR RefSeq; WP_000676549.1; NC_002951.2.
DR AlphaFoldDB; Q5HH35; -.
DR SMR; Q5HH35; -.
DR MEROPS; S01.269; -.
DR PRIDE; Q5HH35; -.
DR EnsemblBacteria; AAW36522; AAW36522; SACOL1057.
DR KEGG; sac:SACOL1057; -.
DR HOGENOM; CLU_073589_1_0_9; -.
DR OMA; NFANDDQ; -.
DR PRO; PR:Q5HH35; -.
DR Proteomes; UP000000530; 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_0000026884"
FT CHAIN 69..336
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000026885"
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 310..312
FT /note="7"
FT REPEAT 313..315
FT /note="8"
FT REPEAT 316..318
FT /note="9"
FT REPEAT 319..321
FT /note="10"
FT REPEAT 322..324
FT /note="11"
FT REGION 34..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..324
FT /note="11 X 3 AA repeats of P-[DN]-N"
FT COMPBIAS 34..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
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 336 AA; 36313 MW; 8B0F7F0C7996AA3E CRC64;
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP 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
PDNPNNPDEP NNPDNPNNPD NPDNGDTNNS DNPDAA
