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Entry: A6NZC1_9FIRM
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Original site: A6NZC1_9FIRM 
ID   A6NZC1_9FIRM            Unreviewed;       559 AA.
AC   A6NZC1;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 93.
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=ptsP {ECO:0000313|EMBL:EDM98770.1};
GN   ORFNames=BACCAP_03572 {ECO:0000313|EMBL:EDM98770.1};
OS   Pseudoflavonifractor capillosus ATCC 29799.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Pseudoflavonifractor.
OX   NCBI_TaxID=411467 {ECO:0000313|EMBL:EDM98770.1, ECO:0000313|Proteomes:UP000003639};
RN   [1] {ECO:0000313|EMBL:EDM98770.1, ECO:0000313|Proteomes:UP000003639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98770.1,
RC   ECO:0000313|Proteomes:UP000003639};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDM98770.1, ECO:0000313|Proteomes:UP000003639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98770.1,
RC   ECO:0000313|Proteomes:UP000003639};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Pseudoflavonifractor capillosus ATCC 29799.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDM98770.1}.
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DR   EMBL; AAXG02000032; EDM98770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6NZC1; -.
DR   STRING; 411467.BACCAP_03572; -.
DR   eggNOG; COG1080; Bacteria.
DR   Proteomes; UP000003639; Unassembled WGS sequence.
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; 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; 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|PIRNR:PIRNR000732, ECO:0000256|PIRSR:PIRSR000732-3};
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:EDM98770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003639};
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          12..110
FT                   /note="Phosphotransferase system enzyme I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05524"
FT   DOMAIN          137..209
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          235..521
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        173
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT   ACT_SITE        486
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT   BINDING         280
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         316
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT   BINDING         438..439
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         439
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT   BINDING         449
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
SQ   SEQUENCE   559 AA;  61887 MW;  D54EB7ABE61C3A0F CRC64;
     MYRFIPYTPL VEQREIAHGE VRTELDRYHR AQAAAREELE TLCRRFSASD QEKTAIFAAH
     LDILMDVAME EDICTAVEDE LVCAEWAVQQ VYGRYAEQIA GAADPLMRER SSDLKDVSRR
     ILRCLEGAED HDLSSLEHAA IVVAHDLLPS QTALLDRDRV LGIAAEIGGS TSHSAIIARS
     YGIPSVLGIE GILDAVQDGE TVILDALKGT LSTQPTHDEL ATAERRKSEY AVKAAELRRW
     RDVPCVMADG TQVGIHLNIG SATPDELSAS MYTDGVGLFR SEFLYMSRPQ LPGEEEQMEA
     YRRALEAFAP RPVVLRTMDI GGDKKLECMD LPREENAFLG SRALRLCFKR KDIFRTQLRA
     AYRASVYGTL WIMFPMVSSV DDIRRAKQIA EEVWQELERE GIPFDREVKL GIMIETPAMA
     VLADRAAKEV DFASIGTNDL CQYALAVDRL NPEVAEYYQS YHPALFRLIG IAGSAFREAG
     KPLGVCGELG GDPLAAPVLV GLGVTKLSMS ASAVAGVKKM LCGLTMEEAR HIAQQAANRS
     TAKKVHRFLE QELGEVLNR
//
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