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PT1_STRSL
ID   PT1_STRSL               Reviewed;         577 AA.
AC   P30299;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000250|UniProtKB:P08839};
DE            EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE   AltName: Full=Phosphotransferase system, enzyme I {ECO:0000250|UniProtKB:P08839};
GN   Name=ptsI;
OS   Streptococcus salivarius.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25975;
RX   PubMed=1427100; DOI=10.1016/0378-1119(92)90163-j;
RA   Gagnon G., Vadeboncoeur C., Levesque R.C., Frenette M.;
RT   "Cloning, sequencing and expression in Escherichia coli of the ptsI gene
RT   encoding enzyme I of the phosphoenolpyruvate:sugar phosphotransferase
RT   transport system from Streptococcus salivarius.";
RL   Gene 121:71-78(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC   STRAIN=ATCC 25975;
RX   PubMed=8294015; DOI=10.1016/0378-1119(93)90443-7;
RA   Gagnon G., Vadeboncoeur C., Frenette M.;
RT   "Phosphotransferase system of Streptococcus salivarius: characterization of
RT   the ptsH gene and its product.";
RL   Gene 136:27-34(1993).
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};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08839}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; M81756; AAA26873.1; -; Genomic_DNA.
DR   EMBL; Z17217; CAA78924.1; -; Genomic_DNA.
DR   PIR; JC1375; JC1375.
DR   RefSeq; WP_002884022.1; NZ_WMYL01000010.1.
DR   AlphaFoldDB; P30299; -.
DR   SMR; P30299; -.
DR   STRING; 1304.HMPREF3219_0201233; -.
DR   PRIDE; P30299; -.
DR   BRENDA; 2.7.3.9; 5952.
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   3: Inferred from homology;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..577
FT                   /note="Phosphoenolpyruvate-protein phosphotransferase"
FT                   /id="PRO_0000147093"
FT   ACT_SITE        191
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   ACT_SITE        506
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         435
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         458..459
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         459
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         469
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
SQ   SEQUENCE   577 AA;  63047 MW;  EDADDF90B85E72D2 CRC64;
     MTEMLKGIAA SDGVAVAKAY LLVQPDLSFE TVTVEDTSAE EARLDAALAA SQDELSVIRE
     KAVESLGEEA AAVFDAHLMV LADPEMTGQI KETIRAKQVN AEAALTEVTD MFIAIFEGME
     DNPYMQERAA DIRDVTKRVL ANLLGKKLPN PATINEESIV VAHDLTPSDT AQLNKKYVKA
     FVTNIGGRTS HSAIMARTLE IAAVLGTNNI TELVKDGDIL AVSGITGEVV INPTEEQIAE
     FKAAGEAYAK QKAEWALLKD AQTVTADGKH FELAANIGTP KDVEGVNDNG AEAVGLYRTE
     FLYMDSQDFP TEDDQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYFDLP KEMNPFLGYR
     ALRISISETG NQMFRTQLRA LLRASVHGKL RIMFPMVALL TEFRTAKGIL EEEKAKLVAE
     GVAVADDIEV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP
     YNPSILRLIN NVIKAAHAEG KWAGMCGEMA GDQTAVPLLV GMGLDEFSMS ATSVLRTRSL
     MKKLDTAKME EYANRALTEC STMEEVLELS KEYVNVD
 
 
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