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 15-DEC-2009, entry version 27. DE RecName: Full=Glutamyl endopeptidase; DE EC=3.4.21.19; DE AltName: Full=Staphylococcal serine proteinase; DE AltName: Full=V8 protease; DE AltName: Full=V8 proteinase; DE AltName: Full=Endoproteinase Glu-C; DE Flags: Precursor; GN Name=sspA; OrderedLocusNames=SAOUHSC_00988; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX MEDLINE=20569178; 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]. RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC8325 genome."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. 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 RT Staphylococcus aureus."; RL Microbiology 150:217-228(2004). RN [4] RP REGULATION. RX MEDLINE=99444917; PubMed=10517329; DOI=10.1007/s004380051090; RA Lindsay J.A., Foster S.J.; RT "Interactive regulatory pathways control virulence determinant RT production and stability in response to environmental conditions in RT Staphylococcus aureus."; RL Mol. Gen. Genet. 262:323-331(1999). RN [5] RP FUNCTION. RX MEDLINE=21340355; PubMed=11447146; RX 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- RT regulation of extracellular proteases."; RL Infect. Immun. 69:4742-4748(2001). RN [6] RP INDUCTION. RX MEDLINE=22112869; PubMed=12117932; RX DOI=10.1128/IAI.70.8.4239-4246.2002; RA Karlsson A., Arvidson S.; RT "Variation in extracellular protease production among clinical RT isolates of Staphylococcus aureus due to different levels of RT expression of the protease repressor sarA."; RL Infect. Immun. 70:4239-4246(2002). RN [7] RP FUNCTION. RX MEDLINE=22289397; PubMed=12207024; DOI=10.1074/jbc.M207162200; RA Massimi I., Park E., Rice K., Mueller-Esterl W., Sauder D., RA McGavin M.J.; RT "Identification of a novel maturation mechanism and restricted RT substrate specificity for the sspB cysteine protease of Staphylococcus RT aureus."; RL J. Biol. Chem. 277:41770-41777(2002). CC -!- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl- CC terminal side of aspartate and glutamate. Along with other CC extracellular proteases it is involved in colonization and CC infection of human tissues. Required for proteolytic maturation of CC thiol protease sspB and inactivation of sspC, an inhibitor of CC sspB. It is the most important protease for degradation of CC fibronectin-binding protein (FnBP) and surface protein A, which CC are involved in adherence to host cells. May also protect bacteria CC against host defense mechanism by cleaving the immunoglobulin CC classes IgG, IgA and IgM. May be involved in the stability of CC secreted lipases. CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa. CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- INDUCTION: Expression occurs in a growth-phase-dependent manner CC with optimal expression at post-exponential phase. Environmental CC conditions such as degree of aeration and salt concentration are CC also important in control of transcription and processing of sspA. CC Up-regulated by agr (accessory gene regulator) and repressed by CC sigmaB factor and sarA. CC -!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage CC leads to the activation of sspA. CC -!- MISCELLANEOUS: The cascade of activation of extracellular CC proteases proceeds from the metalloprotease aureolysin (aur), CC through sspA to sspB. CC -!- SIMILARITY: Belongs to the peptidase S1B family. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="http://www.worthington-biochem.com/STAP/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF309515; AAG45843.1; -; Genomic_DNA. DR EMBL; CP000253; ABD30113.1; -; Genomic_DNA. DR RefSeq; YP_499541.1; -. DR HSSP; Q53782; 2AS9. DR SMR; Q2FZL2; 69-284. DR STRING; Q2FZL2; -. DR GeneID; 3920389; -. DR GenomeReviews; CP000253_GR; SAOUHSC_00988. DR KEGG; sao:SAOUHSC_00988; -. DR HOGENOM; HBG693141; -. DR OMA; EDINFAN; -. DR BioCyc; SAUR93061:SAOUHSC_00988-MON; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR000126; Pept_S1B_AS. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR008256; Peptidase_S1B. DR InterPro; IPR008353; Peptidase_S1B_tx. DR InterPro; IPR009003; Ser/Cys_Pept_Trypsin-like. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR01774; EXFOLTOXIN. DR PRINTS; PR00839; V8PROTEASE. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS00672; V8_HIS; 1. DR PROSITE; PS00673; V8_SER; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Hydrolase; Protease; KW Repeat; Secreted; Serine protease; Signal; Virulence; Zymogen. FT SIGNAL 1 29 Potential. FT PROPEP 30 68 FT /FTId=PRO_0000249327. FT CHAIN 69 336 Glutamyl endopeptidase. FT /FTId=PRO_0000249328. FT REPEAT 289 291 1. FT REPEAT 292 294 2. FT REPEAT 295 297 3. FT REPEAT 298 300 4. FT REPEAT 301 303 5. FT REPEAT 304 306 6. FT REPEAT 310 312 7. FT REPEAT 313 315 8. FT REPEAT 316 318 9. FT REPEAT 319 321 10. FT REPEAT 322 324 11. FT REGION 289 324 11 X 3 AA repeats of P-[DN]-N. FT ACT_SITE 119 119 Charge relay system (By similarity). FT ACT_SITE 161 161 Charge relay system (By similarity). FT ACT_SITE 237 237 Charge relay system (By similarity). FT SITE 68 69 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 //