SSPA_STAAU
ID SSPA_STAAU Reviewed; 336 AA.
AC P0C1U8; P04188;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27733 / V8;
RX PubMed=3306605; DOI=10.1093/nar/15.16.6757;
RA Carmona C., Gray G.L.;
RT "Nucleotide sequence of the serine protease gene of Staphylococcus aureus,
RT strain V8.";
RL Nucleic Acids Res. 15:6757-6757(1987).
RN [2]
RP PROTEIN SEQUENCE OF 69-280.
RC STRAIN=ATCC 27733 / V8;
RX PubMed=96922; DOI=10.1139/o78-082;
RA Drapeau G.R.;
RT "The primary structure of staphylococcal protease.";
RL Can. J. Biochem. 56:534-544(1978).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 27733 / V8;
RX PubMed=4627743; DOI=10.1016/s0021-9258(19)44749-2;
RA Drapeau G.R., Boily Y., Houmard J.;
RT "Purification and properties of an extracellular protease of Staphylococcus
RT aureus.";
RL J. Biol. Chem. 247:6720-6726(1972).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 27733 / V8;
RX PubMed=1372285; DOI=10.1016/0165-2478(92)90124-7;
RA Prokesova L., Potuznikova B., Potempa J., Zikan J., Radl J., Hachova L.,
RA Baran K., Porwit-Bobr Z., John C.;
RT "Cleavage of human immunoglobulins by serine proteinase from Staphylococcus
RT aureus.";
RL Immunol. Lett. 31:259-265(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 69-336.
RC STRAIN=ATCC 27733 / V8;
RA Yamada K., Ohta M., Hasegawa T., Torii K., Murakami M., Kouyama K.;
RT "Crystal structure of an alkaline form of V8 protease from Staphylococcus
RT aureus.";
RL Submitted (JUN-2004) to the PDB data bank.
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:1372285,
CC ECO:0000269|PubMed:4627743}.
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:0000269|PubMed:4627743}.
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; Y00356; CAA68434.1; -; Genomic_DNA.
DR PIR; A26812; PRSASK.
DR RefSeq; WP_000676548.1; NZ_WOFG01000001.1.
DR PDB; 1WCZ; X-ray; 2.00 A; A=69-336.
DR PDBsum; 1WCZ; -.
DR AlphaFoldDB; P0C1U8; -.
DR SMR; P0C1U8; -.
DR IntAct; P0C1U8; 1.
DR BindingDB; P0C1U8; -.
DR ChEMBL; CHEMBL5115; -.
DR MEROPS; S01.269; -.
DR PRIDE; P0C1U8; -.
DR OMA; NFANDDQ; -.
DR EvolutionaryTrace; P0C1U8; -.
DR PRO; PR:P0C1U8; -.
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 3D-structure; Direct protein sequencing; Hydrolase; Protease; 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:96922"
FT /id="PRO_0000026882"
FT CHAIN 69..336
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000026883"
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 ACT_SITE 161
FT /note="Charge relay system"
FT ACT_SITE 237
FT /note="Charge relay system"
FT SITE 68..69
FT /note="Cleavage; by aureolysin"
FT CONFLICT 109
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="V -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 259..261
FT /note="EFN -> QFD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..270
FT /note="ENV -> NEVN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1WCZ"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1WCZ"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1WCZ"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1WCZ"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1WCZ"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:1WCZ"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1WCZ"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:1WCZ"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:1WCZ"
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
