PT1_ENTFA
ID PT1_ENTFA Reviewed; 575 AA.
AC P23530;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:3922407};
DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:3922407};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:3922407};
GN Name=ptsI; OrderedLocusNames=EF_0710;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP PROTEIN SEQUENCE OF 180-208, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE
RP HIS-191, AND SUBUNIT.
RX PubMed=3922407; DOI=10.1021/bi00325a023;
RA Alpert C.-A., Frank R., Stueber K., Deutscher J., Hengstenberg W.;
RT "Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus
RT faecalis: purification and properties of the enzyme and characterization of
RT its active center.";
RL Biochemistry 24:959-964(1985).
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 ECO:0000305|PubMed:3922407}.
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, ECO:0000305|PubMed:3922407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P08839};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3922407}.
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; AE016830; AAO80531.1; -; Genomic_DNA.
DR PIR; A22018; A22018.
DR RefSeq; NP_814461.1; NC_004668.1.
DR RefSeq; WP_010774175.1; NZ_KE136527.1.
DR AlphaFoldDB; P23530; -.
DR SMR; P23530; -.
DR STRING; 226185.EF_0710; -.
DR EnsemblBacteria; AAO80531; AAO80531; EF_0710.
DR KEGG; efa:EF0710; -.
DR PATRIC; fig|226185.45.peg.2652; -.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_7_0_9; -.
DR OMA; CNAEWAL; -.
DR Proteomes; UP000001415; Chromosome.
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 Cytoplasm; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..575
FT /note="Phosphoenolpyruvate-protein phosphotransferase"
FT /id="PRO_0000147068"
FT ACT_SITE 191
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000305|PubMed:3922407"
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 575 AA; 63178 MW; 9A8E709FF128C5AE CRC64;
MSEMLKGIAA SDGVAVAKAY LLVQPDLSFN KTSVEDTDAE ATRLDDALAK STEELQAIRD
KAAQSLGEAE AQVFDAHLMV LSDPEMVGQI KQNIQDNKVN AEAALKEVTD MYIGMFEAMD
DNAYMQERAA DIRDVAKRIL AHLLGVTLPN PSMINEEVIV VAHDLTPSDT AQLDRTYVKA
FVTDIGGRTS HSAIMARSLE IPAIVGTKEI TDKVKAGDIL AVNGIIGDVI IDPTDAEKSE
FEAEAKAYAD QKAEWDKLKN AETVTADGKH VELAANIGTP KDLEGVHKNG GEAVGLYRTE
FLYMDSSDFP TEEDQYQAYK AVLEGMEGKP VVVRTMDIGG DKELPYLTLP HEMNPFLGYR
ALRISLSELG DGMFRTQMRA LLRASVHGNL RIMFPMVATL KEFRAAKAIF EDEKQKLVNE
GVEVSNDIQV GIMIEIPAAA VLADKFAKEV DFFSVGTNDL IQYTMAADRM NERVSYLYQP
YNPSILRLIK NVIDAAHAEG KWAGMCGEMA GDQTAVPLLL GMGLDEFSMS ATSILKTRSL
MKRLDTTKMA ELADRALKEC DTMEEVFALV EEYTK
