PT1P_ECOLI
ID PT1P_ECOLI Reviewed; 748 AA.
AC P37177; Q2MA08;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Phosphoenolpyruvate-dependent phosphotransferase system {ECO:0000303|PubMed:8973315};
DE EC=2.7.3.9 {ECO:0000269|PubMed:10473571};
DE AltName: Full=Enzyme I-Ntr {ECO:0000303|PubMed:8973315};
DE Short=EINtr {ECO:0000303|PubMed:8973315};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:8973315};
GN Name=ptsP; Synonyms=ygdF, ygdO; OrderedLocusNames=b2829, JW2797;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-748.
RX PubMed=7896715; DOI=10.1128/jb.177.7.1879-1882.1995;
RA Gan K., Sankaran K., Williams M.G., Aldea M., Rudd K.E., Kushner S.R.,
RA Wu H.C.;
RT "The umpA gene of Escherichia coli encodes
RT phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and
RT regulates thymidylate synthase levels through translational coupling.";
RL J. Bacteriol. 177:1879-1882(1995).
RN [4]
RP FUNCTION, AND DISCUSSION OF SEQUENCE.
RX PubMed=8973315; DOI=10.1016/s0378-1119(96)00481-7;
RA Reizer J., Reizer A., Merrick M.J., Plunkett G. III, Rose D.J.,
RA Saier M.H. Jr.;
RT "Novel phosphotransferase-encoding genes revealed by analysis of the
RT Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue
RT that possesses a putative sensory transduction domain.";
RL Gene 181:103-108(1996).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=10473571; DOI=10.1074/jbc.274.37.26185;
RA Rabus R., Reizer J., Paulsen I., Saier M.H. Jr.;
RT "Enzyme I(Ntr) from Escherichia coli. A novel enzyme of the
RT phosphoenolpyruvate-dependent phosphotransferase system exhibiting strict
RT specificity for its phosphoryl acceptor, NPr.";
RL J. Biol. Chem. 274:26185-26191(1999).
CC -!- FUNCTION: Component of the phosphoenolpyruvate-dependent nitrogen-
CC metabolic phosphotransferase system (nitrogen-metabolic PTS), that
CC seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr
CC transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the
CC phosphoryl carrier protein (NPr) (PubMed:10473571). Could function in
CC the transcriptional regulation of sigma-54 dependent operons in
CC conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins
CC (PubMed:8973315). Enzyme I-Ntr is specific for NPr (PubMed:10473571).
CC {ECO:0000269|PubMed:10473571, ECO:0000269|PubMed:8973315}.
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:0000269|PubMed:10473571};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10473571};
CC Note=Mn(2+) allows activity only at low concentrations. In the presence
CC of low concentrations of Co(2+) or Ni(2+), activity could be measured,
CC but at concentrations above 0.2 mM, strong inhibition is observed.
CC {ECO:0000269|PubMed:10473571};
CC -!- ACTIVITY REGULATION: Inhibited by GDP and FAD.
CC {ECO:0000269|PubMed:10473571}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for mannitol phosphate {ECO:0000269|PubMed:10473571};
CC Vmax=1 umol/min/mg enzyme {ECO:0000269|PubMed:10473571};
CC Note=Enzyme I-Ntr activity requires high ionic strength.
CC {ECO:0000269|PubMed:10473571};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:10473571};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The EI 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 -!- DOMAIN: The GAF domain is an important site of signal perception in
CC prokaryotes and eukaryotes. {ECO:0000305}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U29581; AAB40476.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75868.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76898.1; -; Genomic_DNA.
DR EMBL; U12289; AAA69023.1; -; Genomic_DNA.
DR PIR; F65065; F65065.
DR RefSeq; NP_417306.1; NC_000913.3.
DR RefSeq; WP_000957910.1; NZ_LN832404.1.
DR PDB; 5T12; X-ray; 2.30 A; A=170-424.
DR PDB; 5T1O; NMR; -; B=170-424.
DR PDBsum; 5T12; -.
DR PDBsum; 5T1O; -.
DR AlphaFoldDB; P37177; -.
DR SASBDB; P37177; -.
DR SMR; P37177; -.
DR BioGRID; 4263274; 26.
DR BioGRID; 851629; 4.
DR IntAct; P37177; 10.
DR STRING; 511145.b2829; -.
DR jPOST; P37177; -.
DR PaxDb; P37177; -.
DR PRIDE; P37177; -.
DR EnsemblBacteria; AAC75868; AAC75868; b2829.
DR EnsemblBacteria; BAE76898; BAE76898; BAE76898.
DR GeneID; 947301; -.
DR KEGG; ecj:JW2797; -.
DR KEGG; eco:b2829; -.
DR PATRIC; fig|1411691.4.peg.3906; -.
DR EchoBASE; EB2105; -.
DR eggNOG; COG3605; Bacteria.
DR HOGENOM; CLU_007308_7_1_6; -.
DR InParanoid; P37177; -.
DR OMA; MFPMISE; -.
DR PhylomeDB; P37177; -.
DR BioCyc; EcoCyc:EG12188-MON; -.
DR BioCyc; MetaCyc:EG12188-MON; -.
DR PRO; PR:P37177; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IDA:EcoCyc.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:EcoCyc.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; 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; PF01590; GAF; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR SMART; SM00065; GAF; 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; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..748
FT /note="Phosphoenolpyruvate-dependent phosphotransferase
FT system"
FT /id="PRO_0000147095"
FT DOMAIN 1..127
FT /note="GAF"
FT /evidence="ECO:0000305|PubMed:8973315"
FT REGION 128..170
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:8973315"
FT REGION 171..748
FT /note="PTS EI"
FT /evidence="ECO:0000305|PubMed:8973315"
FT ACT_SITE 356
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT ACT_SITE 668
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 462
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 498
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 620..621
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 621
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 631
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5T12"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:5T12"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 205..230
FT /evidence="ECO:0007829|PDB:5T12"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 268..284
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 295..309
FT /evidence="ECO:0007829|PDB:5T12"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:5T12"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:5T12"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:5T12"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:5T12"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:5T12"
FT TURN 388..391
FT /evidence="ECO:0007829|PDB:5T12"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:5T12"
FT HELIX 397..410
FT /evidence="ECO:0007829|PDB:5T12"
SQ SEQUENCE 748 AA; 83716 MW; AC7137BD0AEBBF01 CRC64;
MLTRLREIVE KVASAPRLNE ALNILVTDIC LAMDTEVCSV YLADHDRRCY YLMATRGLKK
PRGRTVTLAF DEGIVGLVGR LAEPINLADA QKHPSFKYIP SVKEERFRAF LGVPIIQRRQ
LLGVLVVQQR ELRQYDESEE SFLVTLATQM AAILSQSQLT ALFGQYRQTR IRALPAAPGV
AIAEGWQDAT LPLMEQVYQA STLDPALERE RLTGALEEAA NEFRRYSKRF AAGAQKETAA
IFDLYSHLLS DTRLRRELFA EVDKGSVAEW AVKTVIEKFA EQFAALSDNY LKERAGDLRA
LGQRLLFHLD DANQGPNAWP ERFILVADEL SATTLAELPQ DRLVGVVVRD GAANSHAAIM
VRALGIPTVM GADIQPSVLH RRTLIVDGYR GELLVDPEPV LLQEYQRLIS EEIELSRLAE
DDVNLPAQLK SGERIKVMLN AGLSPEHEEK LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV
AQYQGMLQMF NDKPVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR
AMLRANAATG NLNILLPMVT SLDEVDEARR LIERAGREVE EMIGYEIPKP RIGIMLEVPS
MVFMLPHLAK RVDFISVGTN DLTQYILAVD RNNTRVANIY DSLHPAMLRA LAMIAREAEI
HGIDLRLCGE MAGDPMCVAI LIGLGYRHLS MNGRSVARAK YLLRRIDYAE AENLAQRSLE
AQLATEVRHQ VAAFMERRGM GGLIRGGL
