SSPA_STAAM
ID SSPA_STAAM Reviewed; 342 AA.
AC Q99V45;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=SAV1048;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 69-342.
RX PubMed=14747701; DOI=10.1107/s090744490302599x;
RA Prasad L., Leduc Y., Hayakawa K., Delbaere L.T.J.;
RT "The structure of a universally employed enzyme: V8 protease from
RT Staphylococcus aureus.";
RL Acta Crystallogr. D 60:256-259(2004).
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; BA000017; BAB57210.1; -; Genomic_DNA.
DR RefSeq; WP_000676539.1; NC_002758.2.
DR PDB; 1QY6; X-ray; 1.90 A; A=69-342.
DR PDB; 2O8L; X-ray; 1.50 A; A=69-342.
DR PDBsum; 1QY6; -.
DR PDBsum; 2O8L; -.
DR AlphaFoldDB; Q99V45; -.
DR SMR; Q99V45; -.
DR MEROPS; S01.269; -.
DR PaxDb; Q99V45; -.
DR EnsemblBacteria; BAB57210; BAB57210; SAV1048.
DR KEGG; sav:SAV1048; -.
DR HOGENOM; CLU_073589_1_0_9; -.
DR OMA; NFANDDQ; -.
DR PhylomeDB; Q99V45; -.
DR BioCyc; SAUR158878:SAV_RS05655-MON; -.
DR EvolutionaryTrace; Q99V45; -.
DR PRO; PR:Q99V45; -.
DR Proteomes; UP000002481; 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 3D-structure; Hydrolase; Protease; Repeat; Secreted; Serine protease;
KW Signal; Virulence; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..68
FT /evidence="ECO:0000250"
FT /id="PRO_0000026886"
FT CHAIN 69..342
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000026887"
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 307..309
FT /note="7"
FT REPEAT 310..312
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 REPEAT 325..327
FT /note="12"
FT REPEAT 328..330
FT /note="13"
FT REGION 33..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..330
FT /note="13 X 3 AA repeats of P-[DN]-N"
FT COMPBIAS 33..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..342
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 /evidence="ECO:0000250"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2O8L"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2O8L"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:2O8L"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:2O8L"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2O8L"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:2O8L"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:2O8L"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2O8L"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2O8L"
SQ SEQUENCE 342 AA; 36977 MW; 5AEF42DCE01C4B24 CRC64;
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP KIKKGGNLKP
LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV
VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN
PDNPNNPDNP NNPDEPNNPD NPNNPDNPDN GDNNNSDNPD AA
