PT1_SALTY
ID PT1_SALTY Reviewed; 575 AA.
AC P0A249; P12654;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:1655788};
DE EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:1655788};
DE AltName: Full=Phosphotransferase system, enzyme I {ECO:0000303|PubMed:1655788};
GN Name=ptsI; OrderedLocusNames=STM2432;
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE
RP SITE.
RX PubMed=1655788; DOI=10.1016/s0021-9258(18)55026-2;
RA Licalsi C., Crocenzi T.S., Freire E., Roseman S.;
RT "Sugar transport by the bacterial phosphotransferase system. Structural and
RT thermodynamic domains of enzyme I of Salmonella typhimurium.";
RL J. Biol. Chem. 266:19519-19527(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-299.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=3290198; DOI=10.1128/jb.170.7.3150-3157.1988;
RA Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.;
RT "DNA sequences of the cysK regions of Salmonella typhimurium and
RT Escherichia coli and linkage of the cysK regions to ptsH.";
RL J. Bacteriol. 170:3150-3157(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=2497295; DOI=10.1111/j.1365-2958.1989.tb00110.x;
RA Schnierow B.J., Yamada M., Saier M.H. Jr.;
RT "Partial nucleotide sequence of the pts operon in Salmonella typhimurium:
RT comparative analyses in five bacterial genera.";
RL Mol. Microbiol. 3:113-118(1989).
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:1655788}.
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:1655788};
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; M76176; AAA27060.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21326.1; -; Genomic_DNA.
DR EMBL; M21450; AAA27053.1; -; Genomic_DNA.
DR EMBL; X14737; CAA32867.1; -; Genomic_DNA.
DR PIR; A41027; WQEBPI.
DR RefSeq; NP_461367.1; NC_003197.2.
DR RefSeq; WP_000623114.1; NC_003197.2.
DR AlphaFoldDB; P0A249; -.
DR BMRB; P0A249; -.
DR SMR; P0A249; -.
DR STRING; 99287.STM2432; -.
DR PaxDb; P0A249; -.
DR PRIDE; P0A249; -.
DR EnsemblBacteria; AAL21326; AAL21326; STM2432.
DR GeneID; 1253954; -.
DR KEGG; stm:STM2432; -.
DR PATRIC; fig|99287.12.peg.2570; -.
DR HOGENOM; CLU_007308_7_0_6; -.
DR OMA; CNAEWAL; -.
DR PhylomeDB; P0A249; -.
DR BioCyc; SENT99287:STM2432-MON; -.
DR BRENDA; 2.7.3.9; 5542.
DR SABIO-RK; P0A249; -.
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 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; Kinase; Magnesium; Metal-binding; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..575
FT /note="Phosphoenolpyruvate-protein phosphotransferase"
FT /id="PRO_0000147079"
FT ACT_SITE 189
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08839,
FT ECO:0000305|PubMed:1655788"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 296
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
FT BINDING 332
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 454..455
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08839"
FT BINDING 465
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P23533"
SQ SEQUENCE 575 AA; 63369 MW; 5A87EEE702D823F0 CRC64;
MISGILASPG IAFGKALLLK EDEIVIDRKK ISADKVDQEV ERFLSGRAKA SAQLEAIKTK
AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QATALEELDD
EYLKERAADV RDIGKRLLRN ILGLAIIDLS AIQEEVILVA ADLTPSETAQ LNLQKVLGFI
TDAGGRTSHT SIMARSLELP AIVGTGSVTA QVKNGDYLIL DAVNNQVYVN PTNDVIEQLR
AVQEQVATEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL
FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAV
RIAMDRKEIL RDQVRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF
DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS
VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT
NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKTIC
