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PT1_STAAU
ID   PT1_STAAU               Reviewed;         572 AA.
AC   P51183;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:19801641};
DE            EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE   AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:19801641};
GN   Name=ptsI;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=305A;
RA   Kravanja M., Engelmann R., Christiansen I., Hengstenberg W.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), COFACTOR, ACTIVE SITE, AND SUBUNIT.
RX   PubMed=19801641; DOI=10.1074/jbc.m109.057612;
RA   Oberholzer A.E., Schneider P., Siebold C., Baumann U., Erni B.;
RT   "Crystal structure of enzyme I of the phosphoenolpyruvate sugar
RT   phosphotransferase system in the dephosphorylated state.";
RL   J. Biol. Chem. 284:33169-33176(2009).
CC   -!- FUNCTION: General (non sugar-specific) component of the
CC       phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar
CC       PTS). This major carbohydrate active-transport system catalyzes the
CC       phosphorylation of incoming sugar substrates concomitantly with their
CC       translocation across the cell membrane. Enzyme I transfers the
CC       phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl
CC       carrier protein (HPr). {ECO:0000250|UniProtKB:P08839}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC         L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC         COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC         Evidence={ECO:0000250|UniProtKB:P08839};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:19801641};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19801641}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The N-terminal domain contains the HPr binding site, the
CC       central domain the pyrophosphate/phosphate carrier histidine, and the
CC       C-terminal domain the pyruvate binding site.
CC       {ECO:0000250|UniProtKB:P08839}.
CC   -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC       phosphocarrier histidine residue located on the surface of the central
CC       domain. The two first partial reactions are catalyzed at an active site
CC       located on the N-terminal domain, and the third partial reaction is
CC       catalyzed at an active site located on the C-terminal domain. For
CC       catalytic turnover, the central domain swivels from the concave surface
CC       of the N-terminal domain to that of the C-terminal domain.
CC       {ECO:0000250|UniProtKB:P08839}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR   EMBL; X93205; CAA63689.1; -; Genomic_DNA.
DR   RefSeq; WP_000040054.1; NZ_WOUL01000005.1.
DR   PDB; 2WQD; X-ray; 2.40 A; A=1-572.
DR   PDBsum; 2WQD; -.
DR   AlphaFoldDB; P51183; -.
DR   SMR; P51183; -.
DR   OMA; CNAEWAL; -.
DR   BRENDA; 2.7.3.9; 3352.
DR   EvolutionaryTrace; P51183; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.274.10; -; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR024692; PTS_EI.
DR   InterPro; IPR006318; PTS_EI-like.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR036618; PtsI_HPr-bd_sf.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PIRSF; PIRSF000732; PTS_enzyme_I; 1.
DR   SUPFAM; SSF47831; SSF47831; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Phosphotransferase system; Sugar transport; Transferase; Transport.
FT   CHAIN           1..572
FT                   /note="Phosphoenolpyruvate-protein phosphotransferase"
FT                   /id="PRO_0000147085"
FT   ACT_SITE        191
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P08839,
FT                   ECO:0000305|PubMed:19801641"
FT   ACT_SITE        504
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         298
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
FT   BINDING         334
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         433
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         456..457
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         457
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         467
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
FT   STRAND          3..6
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          8..11
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          13..21
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           38..61
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   TURN            62..66
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           73..81
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           85..98
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           102..118
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           123..143
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          158..163
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           167..170
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   TURN            175..177
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          178..185
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           191..198
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           210..213
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   TURN            224..227
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           235..256
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   TURN            257..260
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          272..279
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           280..282
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           283..288
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           300..303
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          304..308
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           312..325
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   TURN            326..328
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          331..334
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           355..357
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           361..365
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           369..382
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   TURN            383..385
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          388..393
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           398..418
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          427..432
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           435..439
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           441..447
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          449..453
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           455..463
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          467..469
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           470..475
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           481..496
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          500..503
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           506..509
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   TURN            511..513
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           514..520
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   STRAND          524..527
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           529..531
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           532..540
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           544..554
FT                   /evidence="ECO:0007829|PDB:2WQD"
FT   HELIX           560..568
FT                   /evidence="ECO:0007829|PDB:2WQD"
SQ   SEQUENCE   572 AA;  63219 MW;  0CDF16F050CA83DE CRC64;
     MSKLIKGIAA SDGVAIAKAY LLVEPDLTFD KNEKVTDVEG EVAKFNSAIE ASKVELTKIR
     NNAEVQLGAD KAAIFDAHLL VLDDPELIQP IQDKIKNENA NAATALTDVT TQFVTIFESM
     DNEYMKERAA DIRDVSKRVL SHILGVELPN PSMIDESVVI VGNDLTPSDT AQLNKEFVQG
     FATNIGGRTS HSAIMSRSLE IPAIVGTKSI TQEVKQGDMI IVDGLNGDVI VNPTEDELIA
     YQDKRERYFA DKKELQKLRD ADTVTVDGVH AELAANIGTP NDLPGVIENG AQGIGLYRTE
     FLYMGRDQMP TEEEQFEAYK EVLEAMGGKR VVVRTLDIGG DKELSYLNLP EEMNPFLGYR
     AIRLCLAQQD IFRPQLRALL RASVYGKLNI MFPMVATINE FREAKAILLE EKENLKNEGH
     DISDDIELGI MVEIPATAAL ADVFAKEVDF FSIGTNDLIQ YTLAADRMSE RVSYLYQPYN
     PSILRLVKQV IEASHKEGKW TGMCGEMAGD ETAIPLLLGL GLDEFSMSAT SILKARRQIN
     GLSKNEMTEL ANRAVDCATQ EEVIELVNNY VK
 
 
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