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Database: UniProt
Entry: F8HDU1_STRE5
LinkDB: F8HDU1_STRE5
Original site: F8HDU1_STRE5 
ID   F8HDU1_STRE5            Unreviewed;       577 AA.
AC   F8HDU1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000256|ARBA:ARBA00016544, ECO:0000256|PIRNR:PIRNR000732};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232, ECO:0000256|PIRNR:PIRNR000732};
DE   AltName: Full=Phosphotransferase system, enzyme I {ECO:0000256|ARBA:ARBA00033235, ECO:0000256|PIRNR:PIRNR000732};
GN   Name=ptsI {ECO:0000313|EMBL:AEJ53643.1};
GN   OrderedLocusNames=Ssal_01362 {ECO:0000313|EMBL:AEJ53643.1};
OS   Streptococcus salivarius (strain 57.I).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1046629 {ECO:0000313|EMBL:AEJ53643.1, ECO:0000313|Proteomes:UP000000293};
RN   [1] {ECO:0000313|EMBL:AEJ53643.1, ECO:0000313|Proteomes:UP000000293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=57.I {ECO:0000313|EMBL:AEJ53643.1,
RC   ECO:0000313|Proteomes:UP000000293};
RX   PubMed=21914897; DOI=10.1128/JB.05670-11;
RA   Geng J., Huang S.C., Li S., Hu S., Chen Y.Y.;
RT   "Complete genome sequence of the ureolytic Streptococcus salivarius strain
RT   57.I.";
RL   J. Bacteriol. 193:5596-5597(2011).
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:0000256|ARBA:ARBA00002728,
CC       ECO:0000256|PIRNR:PIRNR000732}.
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:0000256|ARBA:ARBA00000683,
CC         ECO:0000256|PIRNR:PIRNR000732};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|PIRSR:PIRSR000732-3};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR000732}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000732}.
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DR   EMBL; CP002888; AEJ53643.1; -; Genomic_DNA.
DR   RefSeq; WP_002884022.1; NC_017594.1.
DR   AlphaFoldDB; F8HDU1; -.
DR   SMR; F8HDU1; -.
DR   KEGG; stf:Ssal_01362; -.
DR   PATRIC; fig|1046629.4.peg.1197; -.
DR   eggNOG; COG1080; Bacteria.
DR   OMA; CNAEWAL; -.
DR   Proteomes; UP000000293; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000732};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000732};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000732};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000732};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683,
KW   ECO:0000256|PIRNR:PIRNR000732}; Pyruvate {ECO:0000313|EMBL:AEJ53643.1};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW   ECO:0000256|PIRNR:PIRNR000732};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000732};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000732}.
FT   DOMAIN          6..128
FT                   /note="Phosphotransferase system enzyme I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05524"
FT   DOMAIN          154..227
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          252..545
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        191
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT   ACT_SITE        506
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT   BINDING         298
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         334
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         435
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT   BINDING         458..459
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         459
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT   BINDING         469
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
SQ   SEQUENCE   577 AA;  63047 MW;  EDADDF90B85E72D2 CRC64;
     MTEMLKGIAA SDGVAVAKAY LLVQPDLSFE TVTVEDTSAE EARLDAALAA SQDELSVIRE
     KAVESLGEEA AAVFDAHLMV LADPEMTGQI KETIRAKQVN AEAALTEVTD MFIAIFEGME
     DNPYMQERAA DIRDVTKRVL ANLLGKKLPN PATINEESIV VAHDLTPSDT AQLNKKYVKA
     FVTNIGGRTS HSAIMARTLE IAAVLGTNNI TELVKDGDIL AVSGITGEVV INPTEEQIAE
     FKAAGEAYAK QKAEWALLKD AQTVTADGKH FELAANIGTP KDVEGVNDNG AEAVGLYRTE
     FLYMDSQDFP TEDDQYEAYK AVLEGMNGKP VVVRTMDIGG DKELPYFDLP KEMNPFLGYR
     ALRISISETG NQMFRTQLRA LLRASVHGKL RIMFPMVALL TEFRTAKGIL EEEKAKLVAE
     GVAVADDIEV GIMIEIPAAA MLADQFAKEV DFFSIGTNDL IQYTMAADRM NEQVSYLYQP
     YNPSILRLIN NVIKAAHAEG KWAGMCGEMA GDQTAVPLLV GMGLDEFSMS ATSVLRTRSL
     MKKLDTAKME EYANRALTEC STMEEVLELS KEYVNVD
//
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