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Database: UniProt
Entry: PT1_BORBU
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Original site: PT1_BORBU 
ID   PT1_BORBU               Reviewed;         573 AA.
AC   O51508;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-NOV-2023, entry version 132.
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=BB_0558;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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. {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; AE000783; AAC66921.1; -; Genomic_DNA.
DR   PIR; E70169; E70169.
DR   RefSeq; NP_212692.1; NC_001318.1.
DR   RefSeq; WP_002656738.1; NC_001318.1.
DR   AlphaFoldDB; O51508; -.
DR   SMR; O51508; -.
DR   STRING; 224326.BB_0558; -.
DR   PaxDb; 224326-BB_0558; -.
DR   EnsemblBacteria; AAC66921; AAC66921; BB_0558.
DR   GeneID; 56567990; -.
DR   KEGG; bbu:BB_0558; -.
DR   PATRIC; fig|224326.49.peg.949; -.
DR   HOGENOM; CLU_007308_7_0_12; -.
DR   OMA; CNAEWAL; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000001807; 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; 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; 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   3: Inferred from homology;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transport.
FT   CHAIN           1..573
FT                   /note="Phosphoenolpyruvate-protein phosphotransferase"
FT                   /id="PRO_0000147060"
FT   ACT_SITE        190
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   ACT_SITE        504
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         297
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
FT   BINDING         334
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         433
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         456..457
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         457
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         467
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
SQ   SEQUENCE   573 AA;  64595 MW;  BB073793270BED45 CRC64;
     MTLSGKRISK GIGIGEVLCI RKNFDKIISR EKIDFSQVDS EISKFNKAKS KAIEALRDLE
     RKAMLQFGDD KKGIFEGQVL IVEDDELDEL VIELIVKENY SAAYSIYLAF ENLVKSVEDY
     KDPYLKERAS DYKDIRNRLI SIILGQVSDF SEINKDIILV TEELTPSDTM QFDLNYVKGF
     LTAVGGETSH AAILARTMGL PALVMTLSDI DALKDGDKIV IDAMSSIVIK NPSSDEINLY
     EGKILRQVEL EKELFSLKDK DAETKDGTKV FLKANIGTPV DITYVNKYGV EGIGLFRTEF
     LYMRSLQPPT EDEQFETYKR VIETMEKKGV VTIRTLDVGG DKEIPYLNFK KEENPFLGFR
     ALRMYKEYEE LIQAQFNAIF RASHYGKIRV MVPMLTIYEE IETIEYFVNN AKINLKSRGL
     PFDENLEVGC MIEVPSAALI SSKLANKLKF FSIGTNDLTQ YVLAVDRGNQ KISNLYDKYN
     PAVLKLIKKV LDDGVSSGID VSVCGELGGD DAGALLLVGL GFRSLSMIPS ATLRIKYLLK
     KYTIMELEEL ANKVLNSDSK QETLSYFDKF IGD
//
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