SSPA_STAA8
ID SSPA_STAA8 Reviewed; 336 AA.
AC Q2FZL2; P04188;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SAOUHSC_00988;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11119502; DOI=10.1128/iai.69.1.159-169.2001;
RA Rice K., Peralta R., Bast D., de Azavedo J., McGavin M.J.;
RT "Description of Staphylococcus serine protease (ssp) operon in
RT Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine
RT protease.";
RL Infect. Immun. 69:159-169(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP PROTEIN SEQUENCE OF 69-76, FUNCTION, AND INDUCTION.
RX PubMed=14702415; DOI=10.1099/mic.0.26634-0;
RA Shaw L., Golonka E., Potempa J., Foster S.J.;
RT "The role and regulation of the extracellular proteases of Staphylococcus
RT aureus.";
RL Microbiology 150:217-228(2004).
RN [4]
RP REGULATION.
RX PubMed=10517329; DOI=10.1007/s004380051090;
RA Lindsay J.A., Foster S.J.;
RT "Interactive regulatory pathways control virulence determinant production
RT and stability in response to environmental conditions in Staphylococcus
RT aureus.";
RL Mol. Gen. Genet. 262:323-331(1999).
RN [5]
RP FUNCTION.
RX PubMed=11447146; DOI=10.1128/iai.69.8.4742-4748.2001;
RA Karlsson A., Saravia-Otten P., Tegmark K., Morfeldt E., Arvidson S.;
RT "Decreased amounts of cell wall-associated protein A and fibronectin-
RT binding proteins in Staphylococcus aureus sarA mutants due to up-regulation
RT of extracellular proteases.";
RL Infect. Immun. 69:4742-4748(2001).
RN [6]
RP INDUCTION.
RX PubMed=12117932; DOI=10.1128/iai.70.8.4239-4246.2002;
RA Karlsson A., Arvidson S.;
RT "Variation in extracellular protease production among clinical isolates of
RT Staphylococcus aureus due to different levels of expression of the protease
RT repressor sarA.";
RL Infect. Immun. 70:4239-4246(2002).
RN [7]
RP FUNCTION.
RX PubMed=12207024; DOI=10.1074/jbc.m207162200;
RA Massimi I., Park E., Rice K., Mueller-Esterl W., Sauder D., McGavin M.J.;
RT "Identification of a novel maturation mechanism and restricted substrate
RT specificity for the sspB cysteine protease of Staphylococcus aureus.";
RL J. Biol. Chem. 277:41770-41777(2002).
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. {ECO:0000269|PubMed:11119502,
CC ECO:0000269|PubMed:11447146, ECO:0000269|PubMed:12207024,
CC ECO:0000269|PubMed:14702415}.
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 -!- INDUCTION: Expression occurs in a growth-phase-dependent manner with
CC optimal expression at post-exponential phase. Environmental conditions
CC such as degree of aeration and salt concentration are also important in
CC control of transcription and processing of SspA. Up-regulated by Agr
CC (accessory gene regulator) and repressed by sigmaB factor and SarA.
CC {ECO:0000269|PubMed:12117932, ECO:0000269|PubMed:14702415}.
CC -!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads
CC to the activation of SspA.
CC -!- MISCELLANEOUS: The cascade of activation of extracellular proteases
CC proceeds from the metalloprotease aureolysin (aur), through SspA to
CC SspB.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/STAP/";
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DR EMBL; AF309515; AAG45843.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30113.1; -; Genomic_DNA.
DR RefSeq; WP_000676548.1; NZ_LS483365.1.
DR RefSeq; YP_499541.1; NC_007795.1.
DR AlphaFoldDB; Q2FZL2; -.
DR SMR; Q2FZL2; -.
DR STRING; 1280.SAXN108_1046; -.
DR MEROPS; S01.269; -.
DR PRIDE; Q2FZL2; -.
DR EnsemblBacteria; ABD30113; ABD30113; SAOUHSC_00988.
DR GeneID; 3920389; -.
DR KEGG; sao:SAOUHSC_00988; -.
DR PATRIC; fig|93061.5.peg.908; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_073589_1_0_9; -.
DR OMA; NFANDDQ; -.
DR BRENDA; 3.4.21.19; 3352.
DR BRENDA; 3.4.24.29; 3352.
DR PRO; PR:Q2FZL2; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Virulence; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..68
FT /evidence="ECO:0000269|PubMed:14702415"
FT /id="PRO_0000249327"
FT CHAIN 69..336
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000249328"
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"
SQ SEQUENCE 336 AA; 36326 MW; 8B138D0C7996AA3E 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 NPDNGDNNNS DNPDAA
