ID   PT1P_SALTY              Reviewed;         748 AA.
AC   P37178;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   02-SEP-2026, entry version 156.
DE   RecName: Full=Phosphoenolpyruvate-dependent phosphotransferase system {ECO:0000250|UniProtKB:P37177};
DE            EC=2.7.3.9 {ECO:0000250|UniProtKB:P37177};
DE   AltName: Full=Enzyme I-Ntr {ECO:0000250|UniProtKB:P37177};
DE            Short=EINtr {ECO:0000250|UniProtKB:P37177};
DE   AltName: Full=Phosphotransferase system, enzyme I;
GN   Name=ptsP; OrderedLocusNames=STM3003;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 664-748.
RC   STRAIN=LT2;
RX   PubMed=8344935; DOI=10.1016/s0021-9258(19)85453-4;
RA   Gan K., Gupta S.D., Sankaran K., Schmid M.B., Wu H.C.;
RT   "Isolation and characterization of a temperature-sensitive mutant of
RT   Salmonella typhimurium defective in prolipoprotein modification.";
RL   J. Biol. Chem. 268:16544-16550(1993).
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). Could function in the transcriptional
CC       regulation of sigma-54 dependent operons in conjunction with the NPr
CC       (PtsO) and EIIA-Ntr (PtsN) proteins. Enzyme I-Ntr is specific for NPr.
CC       {ECO:0000250|UniProtKB:P37177}.
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:P37177};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P37177};
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:0000250|UniProtKB:P37177}.
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; AE006468; AAL21879.1; -; Genomic_DNA.
DR   EMBL; L13259; AAA20895.1; -; Genomic_DNA.
DR   PIR; B47354; B47354.
DR   RefSeq; NP_461920.1; NC_003197.2.
DR   RefSeq; WP_000957887.1; NC_003197.2.
DR   AlphaFoldDB; P37178; -.
DR   SMR; P37178; -.
DR   STRING; 99287.STM3003; -.
DR   PaxDb; 99287-STM3003; -.
DR   GeneID; 1254526; -.
DR   KEGG; stm:STM3003; -.
DR   PATRIC; fig|99287.12.peg.3178; -.
DR   HOGENOM; CLU_007308_7_1_6; -.
DR   OMA; IYLADHD; -.
DR   PhylomeDB; P37178; -.
DR   BioCyc; SENT99287:STM3003-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; ISS:UniProtKB.
DR   GO; GO:0015764; P:N-acetylglucosamine transport; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   FunFam; 1.10.274.10:FF:000002; Phosphoenolpyruvate-protein phosphotransferase PtsP; 1.
DR   FunFam; 3.20.20.60:FF:000012; Phosphoenolpyruvate-protein phosphotransferase PtsP; 1.
DR   FunFam; 3.30.450.40:FF:000012; Phosphoenolpyruvate-protein phosphotransferase PtsP; 1.
DR   FunFam; 3.50.30.10:FF:000003; Phosphoenolpyruvate-protein phosphotransferase ptsP; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR050499; PEP-utilizing_PTS_enzyme.
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   NCBIfam; NF008283; PRK11061.1; 1.
DR   NCBIfam; TIGR01417; PTS_I_fam; 1.
DR   PANTHER; PTHR46244:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
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   PRINTS; PR01736; PHPHTRNFRASE.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS50813; GAF; 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   Reference proteome; Sugar transport; Transferase; Transport.
FT   CHAIN           1..748
FT                   /note="Phosphoenolpyruvate-dependent phosphotransferase
FT                   system"
FT                   /id="PRO_0000147096"
FT   DOMAIN          1..155
FT                   /note="GAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01434"
FT   REGION          128..170
FT                   /note="Linker"
FT                   /evidence="ECO:0000250|UniProtKB:P37177"
FT   REGION          171..748
FT                   /note="PTS EI"
FT                   /evidence="ECO:0000250|UniProtKB:P37177"
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"
SQ   SEQUENCE   748 AA;  83627 MW;  46799C4447B75189 CRC64;
     MLTRLREIVE KVASAPRLNE ALNILVTDIC LAMDTEVCSV YLADHDRRCY YLMATRGLKK
     PRGRTVALAF DEGIVGLVGR LAEPINLADA QKHPSFKYIP SVKEERFRAF LGVPIIQRRQ
     LLGVLVVQQR ELRQYDESEE SFLVTLATQM AAILSQSQVT ALFGQYRQTR IRALPAAPGV
     AIATGWQDAT MPLMEQVYEA STLDTSLERE RLTGALEEAA NEFRRYSKRF AAGAQKETAA
     IFDLYSHLLS DARLRRELFA EVDKGAVAEW AVKKIIEKFA EQFAALTDNY LKERAGDLRT
     LGQRLLFHLD DSVQGPNAWP ERFILVADEL SATTLAELPQ DRLAGVVVRD GAANSHAAIM
     VRALGIPTVM GADIQPSVLH RRTLVVDGYR GELLVDPEPV LIQEYQRLIS EEIELSRLAE
     DDVNLPAQLK SGERVKVMLN AGLSPEHEEK LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV
     AQYQGMLQMF NDKPVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLIQVR
     AMLRANAATG NLSILLPMVT SIDEVDEARR LIERAGREVE EMIGYAIPKP RIGIMLEVPS
     MVFMLPHLAN RIDFISVGTN DLTQYILAVD RNNTRVASIY DSLHPAMLRA LSMIAQEAEK
     HGLDLRLCGE MAGDPMCVAI LIGLGYRHLS MNGRSVARVK YLLRHIDFED AQTLARRSLE
     AQMATEVRHQ VAAFMERRGM GGLIRGGL
//