PT1P_SALTY
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 03-AUG-2022, entry version 141.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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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; P37178; -.
DR EnsemblBacteria; AAL21879; AAL21879; STM3003.
DR GeneID; 1254526; -.
DR KEGG; stm:STM3003; -.
DR PATRIC; fig|99287.12.peg.3178; -.
DR HOGENOM; CLU_007308_7_1_6; -.
DR OMA; MFPMISE; -.
DR PhylomeDB; P37178; -.
DR BioCyc; SENT99287:STM3003-MON; -.
DR Proteomes; UP000001014; 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 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 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..127
FT /note="GAF"
FT /evidence="ECO:0000250|UniProtKB:P37177"
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
