PT1_BACSU
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 03-AUG-2022, entry version 157.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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; NZ_JNCM01000035.1.
DR AlphaFoldDB; P08838; -.
DR SMR; P08838; -.
DR IntAct; P08838; 4.
DR MINT; P08838; -.
DR STRING; 224308.BSU13910; -.
DR jPOST; P08838; -.
DR PaxDb; P08838; -.
DR PRIDE; P08838; -.
DR EnsemblBacteria; CAB13264; CAB13264; BSU_13910.
DR GeneID; 64303279; -.
DR GeneID; 939253; -.
DR KEGG; bsu:BSU13910; -.
DR PATRIC; fig|224308.179.peg.1517; -.
DR eggNOG; COG1080; Bacteria.
DR InParanoid; P08838; -.
DR OMA; MFPMISE; -.
DR PhylomeDB; P08838; -.
DR BioCyc; BSUB:BSU13910-MON; -.
DR BRENDA; 2.7.3.9; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; 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; 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
