ID   PT1_BACSU               Reviewed;         570 AA.
AC   P08838; O31692;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   04-NOV-2026, entry version 174.
DE   RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000250|UniProtKB:P08839};
DE            EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE   AltName: Full=Phosphotransferase system, enzyme I {ECO:0000250|UniProtKB:P08839};
GN   Name=ptsI; OrderedLocusNames=BSU13910;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7686067; DOI=10.1002/pro.5560020403;
RA   Reizer J., Hoischen C., Reizer A., Pham T.N., Saier M.H. Jr.;
RT   "Sequence analyses and evolutionary relationships among the energy-coupling
RT   proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar
RT   phosphotransferase system.";
RL   Protein Sci. 2:506-521(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Reizer J.;
RL   Submitted (MAR-1997) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
RC   STRAIN=168;
RX   PubMed=2497294; DOI=10.1111/j.1365-2958.1989.tb00109.x;
RA   Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M.;
RT   "Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis:
RT   nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a
RT   ptsHI operon.";
RL   Mol. Microbiol. 3:103-112(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 398-570.
RC   STRAIN=168;
RX   PubMed=8449881; DOI=10.1128/jb.175.6.1735-1744.1993;
RA   Fajardo-Cavazos P., Salazar C., Nicholson W.L.;
RT   "Molecular cloning and characterization of the Bacillus subtilis spore
RT   photoproduct lyase (spl) gene, which is involved in repair of UV radiation-
RT   induced DNA damage during spore germination.";
RL   J. Bacteriol. 175:1735-1744(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-13.
RX   PubMed=1495386; DOI=10.1111/j.1365-2958.1992.tb00882.x;
RA   Mitchell C., Morris P.W., Vary J.C.;
RT   "Amino acid sequences of several Bacillus subtilis proteins modified by
RT   apparent guanylylation.";
RL   Mol. Microbiol. 6:1579-1581(1992).
RN   [8]
RP   INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=23651456; DOI=10.1111/mmi.12252;
RA   Bach J.N., Bramkamp M.;
RT   "Flotillins functionally organize the bacterial membrane.";
RL   Mol. Microbiol. 88:1205-1217(2013).
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   -!- 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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P08839};
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with FloT
CC       (PubMed:23651456). {ECO:0000250|UniProtKB:P08839,
CC       ECO:0000269|PubMed:23651456}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane raft
CC       {ECO:0000269|PubMed:23651456}. Note=Present in detergent-resistant
CC       membrane (DRM) fractions that may be equivalent to eukaryotic membrane
CC       rafts; these rafts include proteins involved in signaling, molecule
CC       trafficking and protein secretion. {ECO:0000269|PubMed:23651456}.
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; M98359; AAB52374.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13264.2; -; Genomic_DNA.
DR   EMBL; X12832; CAA31318.1; -; Genomic_DNA.
DR   EMBL; L08809; AAA22414.1; -; Genomic_DNA.
DR   PIR; C46238; C46238.
DR   RefSeq; NP_389274.2; NC_000964.3.
DR   RefSeq; WP_003218638.1; NC_000964.3.
DR   AlphaFoldDB; P08838; -.
DR   SMR; P08838; -.
DR   FunCoup; P08838; 515.
DR   IntAct; P08838; 4.
DR   STRING; 224308.BSU13910; -.
DR   jPOST; P08838; -.
DR   PaxDb; 224308-BSU13910; -.
DR   EnsemblBacteria; CAB13264; CAB13264; BSU_13910.
DR   GeneID; 306026897; -.
DR   GeneID; 939253; -.
DR   KEGG; bsu:BSU13910; -.
DR   PATRIC; fig|224308.179.peg.1517; -.
DR   eggNOG; COG1080; Bacteria.
DR   InParanoid; P08838; -.
DR   OMA; AADRMCG; -.
DR   OrthoDB; 9765468at2; -.
DR   PhylomeDB; P08838; -.
DR   BioCyc; BSUB:BSU13910-MONOMER; -.
DR   BRENDA; 2.7.3.9; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P08838; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; EXP:UniProtKB.
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:000001; Phosphoenolpyruvate-protein phosphotransferase; 1.
DR   FunFam; 3.20.20.60:FF:000007; Phosphoenolpyruvate-protein phosphotransferase; 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; 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; 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   NCBIfam; TIGR01417; PTS_I_fam; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
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   PRINTS; PR01736; PHPHTRNFRASE.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 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; Membrane;
KW   Metal-binding; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..570
FT                   /note="Phosphoenolpyruvate-protein phosphotransferase"
FT                   /id="PRO_0000147059"
FT   ACT_SITE        189
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
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   570 AA;  63079 MW;  86163CD5639F3369 CRC64;
     MQELKGIGAS AGIAIAKAYR LEEPDLTVEK KNISDSEAEV SRFDEAIARS KEELEKIKEH
     ALKELGQDKA DIFSAHLLVL SDPELLNPVK EKISTDSVNA EFALKETSSM FVTMFESMDN
     EYMKERAADI RDVTKRVTGH LLGVEIPNPS MISEEVIIVA EDLTPSDTAQ LNREFVKGFT
     TDIGGRTSHS AIMARSLEIP AVVGTKAATG TIQNGVTVIV DGINGDVIID PSAETVKEYE
     EKHNAYLAQK AEWAKLVNEP TVSKDGHHVE LAANIGTPDD VKGVLENGGE AVGLYRTEFL
     YMGRDQLPTE DEQFDAYKTV LERMEGKSVV VRTLDIGGDK ELPYLQLPKE MNPFLGYRAI
     RLCLEEQEIF RTQLRALLRA STYGNLKIMF PMIATVNEFK EAKAILLEEK EKLVKAGQAV
     SDDIEVGMMV EIPSTAVIAD QFAKEVDFFS IGTNDLIQYT MAADRMNERV SYLYQPYNPA
     ILRLITLVIE AAHKEGKWVG MCGEMAGDEI AIPILLGLGL DEFSMSATSI LPARTQISKL
     SKQEAESFKE KILSMSTTEE VVAFVKETFK
//