(data stored in ACNUC9435 zone)

SWISSPROT: PT1_LISIN

ID   PT1_LISIN               Reviewed;         572 AA.
AC   Q92D19;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 111.
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=lin1002;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
DR   EMBL; AL596167; CAC96233.1; -; Genomic_DNA.
DR   PIR; AI1557; AI1557.
DR   RefSeq; WP_003761534.1; NC_003212.1.
DR   SMR; Q92D19; -.
DR   STRING; 272626.lin1002; -.
DR   EnsemblBacteria; CAC96233; CAC96233; CAC96233.
DR   KEGG; lin:lin1002; -.
DR   eggNOG; ENOG4105BZ3; Bacteria.
DR   eggNOG; COG1080; LUCA.
DR   HOGENOM; HOG000278513; -.
DR   KO; K08483; -.
DR   OMA; CNAEWAL; -.
DR   OrthoDB; 467393at2; -.
DR   BioCyc; GCF_000195795:LIN_RS05120-MONOMER; -.
DR   Proteomes; UP000002513; 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   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   3: Inferred from homology;
DR   PRODOM; Q92D19.
DR   SWISS-2DPAGE; Q92D19.
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..572
FT                   /note="Phosphoenolpyruvate-protein phosphotransferase"
FT                   /id="PRO_0000147073"
FT   REGION          455..456
FT                   /note="PEP binding"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   ACT_SITE        190
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   ACT_SITE        503
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   METAL           432
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   METAL           456
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         297
FT                   /note="PEP"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
FT   BINDING         333
FT                   /note="PEP"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         466
FT                   /note="PEP"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
SQ   SEQUENCE   572 AA;  63194 MW;  ECE7E3BD60BCE193 CRC64;
     MAKELKGIAA SDGIAIAKAY LLVEPDLSYE KTEVTDVESE VKRFESALEV SRTELSTIRE
     KAAKDLGEDK AQIFDAHLLV LNDPELTGPI EESIKNAKTN AETALQETTD MFIGMFESMD
     NEYMRERAAD IKDVRKRVLS HLLGVTIPNP ALIDEEVVVV AADLTPSDTA QLNRKFVKGF
     VTDIGGRTSH SAIMARSLEI PAVVGTKEVT ASVAKNDIVI IDGLEGNVII HPTEEQIAHY
     EKIKSDFALQ QAEWEKLKNE KTVSKDGVHV ELAANIGTPN DLEGVISNGG EAVGLYRTEF
     LYMGRDNFPT EEEQFEAYKA VVSGMDGKSV VVRTLDIGGD KTLPYLELPE EMNPFLGFRA
     IRLCFANEEL FRTQLRALLR ASVYGNLKIM FPMIATVNEF RQARDILLDE KAKLKAAGTE
     VSDSIELGIM IEIPAAAVLA DQFAKEVDFF SIGTNDLIQY TMAADRMNER VSYLYQPYNP
     SILRLVKMVI DASHKEGKWT GMCGEMAGDQ TAVPLLLGLG LDEFSMSASS ILKSRSLIKR
     LDQSEMVKLA EEALNKSTAE EVVELVEKYT AE
//

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