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Glutamyl endopeptidase (EC 3.4.21.19) (Endoproteinase Glu-C) (Staphylococcal serine proteinase) (V8 protease) (V8 proteinase)

 SSPA_STAAU              Reviewed;         336 AA.
P0C1U8; P04188;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
23-MAY-2018, entry version 68.
RecName: Full=Glutamyl endopeptidase;
EC=3.4.21.19;
AltName: Full=Endoproteinase Glu-C;
AltName: Full=Staphylococcal serine proteinase;
AltName: Full=V8 protease;
AltName: Full=V8 proteinase;
Flags: Precursor;
Name=sspA;
Staphylococcus aureus.
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=1280;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 27733 / V8;
PubMed=3306605; DOI=10.1093/nar/15.16.6757;
Carmona C., Gray G.L.;
"Nucleotide sequence of the serine protease gene of Staphylococcus
aureus, strain V8.";
Nucleic Acids Res. 15:6757-6757(1987).
[2]
PROTEIN SEQUENCE OF 69-280.
STRAIN=ATCC 27733 / V8;
PubMed=96922;
Drapeau G.R.;
"The primary structure of staphylococcal protease.";
Can. J. Biochem. 56:534-544(1978).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 27733 / V8;
PubMed=4627743;
Drapeau G.R., Boily Y., Houmard J.;
"Purification and properties of an extracellular protease of
Staphylococcus aureus.";
J. Biol. Chem. 247:6720-6726(1972).
[4]
FUNCTION.
STRAIN=ATCC 27733 / V8;
PubMed=1372285; DOI=10.1016/0165-2478(92)90124-7;
Prokesova L., Potuznikova B., Potempa J., Zikan J., Radl J.,
Hachova L., Baran K., Porwit-Bobr Z., John C.;
"Cleavage of human immunoglobulins by serine proteinase from
Staphylococcus aureus.";
Immunol. Lett. 31:259-265(1992).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 69-336.
STRAIN=ATCC 27733 / V8;
Yamada K., Ohta M., Hasegawa T., Torii K., Murakami M., Kouyama K.;
"Crystal structure of an alkaline form of V8 protease from
Staphylococcus aureus.";
Submitted (JUN-2004) to the PDB data bank.
-!- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-
terminal side of aspartate and glutamate. Along with other
extracellular proteases it is involved in colonization and
infection of human tissues. Required for proteolytic maturation of
thiol protease SspB and inactivation of SspC, an inhibitor of
SspB. It is the most important protease for degradation of
fibronectin-binding protein (FnBP) and surface protein A, which
are involved in adherence to host cells. May also protect bacteria
against host defense mechanism by cleaving the immunoglobulin
classes IgG, IgA and IgM. May be involved in the stability of
secreted lipases. {ECO:0000269|PubMed:1372285,
ECO:0000269|PubMed:4627743}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
{ECO:0000255|PROSITE-ProRule:PRU10083}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4627743}.
-!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage
leads to the activation of SspA.
-!- MISCELLANEOUS: The cascade of activation of extracellular
proteases proceeds from the metalloprotease aureolysin (aur),
through SspA to SspB.
-!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/STAP/";
-----------------------------------------------------------------------
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EMBL; Y00356; CAA68434.1; -; Genomic_DNA.
PIR; A26812; PRSASK.
RefSeq; WP_000676548.1; NZ_PQBI01000002.1.
PDB; 1WCZ; X-ray; 2.00 A; A=69-336.
PDBsum; 1WCZ; -.
ProteinModelPortal; P0C1U8; -.
SMR; P0C1U8; -.
IntAct; P0C1U8; 1.
BindingDB; P0C1U8; -.
ChEMBL; CHEMBL5115; -.
MEROPS; S01.269; -.
PRIDE; P0C1U8; -.
eggNOG; ENOG4108CHM; Bacteria.
eggNOG; COG3591; LUCA.
EvolutionaryTrace; P0C1U8; -.
PRO; PR:P0C1U8; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR008256; Peptidase_S1B.
InterPro; IPR008353; Peptidase_S1B_tx.
InterPro; IPR028301; V8_his_AS.
InterPro; IPR000126; V8_ser_AS.
PRINTS; PR01774; EXFOLTOXIN.
PRINTS; PR00839; V8PROTEASE.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS00672; V8_HIS; 1.
PROSITE; PS00673; V8_SER; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Hydrolase; Protease; Repeat;
Secreted; Serine protease; Signal; Virulence; Zymogen.
SIGNAL 1 29 {ECO:0000255}.
PROPEP 30 68 {ECO:0000269|PubMed:96922}.
/FTId=PRO_0000026882.
CHAIN 69 336 Glutamyl endopeptidase.
/FTId=PRO_0000026883.
REPEAT 289 291 1.
REPEAT 292 294 2.
REPEAT 295 297 3.
REPEAT 298 300 4.
REPEAT 301 303 5.
REPEAT 304 306 6.
REPEAT 310 312 7.
REPEAT 313 315 8.
REPEAT 316 318 9.
REPEAT 319 321 10.
REPEAT 322 324 11.
REGION 289 324 11 X 3 AA repeats of P-[DN]-N.
ACT_SITE 119 119 Charge relay system.
ACT_SITE 161 161 Charge relay system.
ACT_SITE 237 237 Charge relay system.
SITE 68 69 Cleavage; by aureolysin.
CONFLICT 109 109 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 125 125 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 145 145 N -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 193 193 V -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 229 229 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 259 261 EFN -> QFD (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 268 270 ENV -> NEVN (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 75 80 {ECO:0000244|PDB:1WCZ}.
HELIX 85 87 {ECO:0000244|PDB:1WCZ}.
STRAND 90 96 {ECO:0000244|PDB:1WCZ}.
STRAND 101 108 {ECO:0000244|PDB:1WCZ}.
STRAND 110 116 {ECO:0000244|PDB:1WCZ}.
HELIX 118 121 {ECO:0000244|PDB:1WCZ}.
HELIX 122 124 {ECO:0000244|PDB:1WCZ}.
HELIX 128 130 {ECO:0000244|PDB:1WCZ}.
STRAND 131 135 {ECO:0000244|PDB:1WCZ}.
STRAND 148 155 {ECO:0000244|PDB:1WCZ}.
STRAND 157 160 {ECO:0000244|PDB:1WCZ}.
STRAND 163 167 {ECO:0000244|PDB:1WCZ}.
HELIX 176 179 {ECO:0000244|PDB:1WCZ}.
STRAND 196 201 {ECO:0000244|PDB:1WCZ}.
STRAND 211 222 {ECO:0000244|PDB:1WCZ}.
STRAND 225 230 {ECO:0000244|PDB:1WCZ}.
STRAND 240 242 {ECO:0000244|PDB:1WCZ}.
STRAND 248 256 {ECO:0000244|PDB:1WCZ}.
TURN 257 259 {ECO:0000244|PDB:1WCZ}.
STRAND 260 265 {ECO:0000244|PDB:1WCZ}.
HELIX 268 277 {ECO:0000244|PDB:1WCZ}.
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


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