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Database: UniProt
Entry: L5NBY6_9BACI
LinkDB: L5NBY6_9BACI
Original site: L5NBY6_9BACI 
ID   L5NBY6_9BACI            Unreviewed;       571 AA.
AC   L5NBY6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
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   ORFNames=D479_04543 {ECO:0000313|EMBL:ELK47997.1};
OS   Halobacillus sp. BAB-2008.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK47997.1, ECO:0000313|Proteomes:UP000010769};
RN   [1] {ECO:0000313|EMBL:ELK47997.1, ECO:0000313|Proteomes:UP000010769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK47997.1,
RC   ECO:0000313|Proteomes:UP000010769};
RX   PubMed=23469348;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT   BAB-2008.";
RL   Genome Announc. 1:E00222-12(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: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:ELK47997.1}.
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DR   EMBL; ANPF01000014; ELK47997.1; -; Genomic_DNA.
DR   RefSeq; WP_008634106.1; NZ_ANPF01000014.1.
DR   AlphaFoldDB; L5NBY6; -.
DR   PATRIC; fig|1246484.3.peg.948; -.
DR   eggNOG; COG1080; Bacteria.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000010769; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010769};
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          5..126
FT                   /note="Phosphotransferase system enzyme I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05524"
FT   DOMAIN          152..225
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          250..540
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        189
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT   ACT_SITE        502
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-1"
FT   BINDING         296
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         332
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         431
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT   BINDING         454..455
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
FT   BINDING         455
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-3"
FT   BINDING         465
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000732-2"
SQ   SEQUENCE   571 AA;  63589 MW;  696732CAE2FA12FE CRC64;
     MTQLQGIAAS SGIAIAKVYR LEAPDLSFTK NDIEQPEEEV KRLHEALNTS KSELEKIKEH
     TKKSLGDEHA EIFSAHLLVL SDPELIQPVE DKIKSDNVNA EFALSETADM FINMFESMDN
     EYMRERAADI RDVTKRVMAH LLGVTFPDPA LINEEVVIVA DDLTPSDTAQ LNKQYVKGFT
     TDIGGRTSHS AIMARSLEIP AVVGTKNITS QADKDTMIIV DGISGDVIID PSDEQIAAYK
     QKQDDFEKQK QEWAKLKDEP TITSEGEHVE LVANIGTPED VEGVLNNGGE GVGLYRTEFL
     YMGKSQLPTE EEQYDAYSSV LKQMGDKPVV VRTLDIGGDK ELDYLELPHE MNPFLGYRAI
     RLCLERDDIF RVQLRALLRA SVHGNLKIMF PMIATLDEFR QAKALLEEEK ANLVKEGQEV
     SDDIEVGMMV EIPATAVIAR QFAKEVDFFS IGTNDLIQYT MAADRMNERV SYLYQPYNPA
     ILNLINNVIE AAHAEGKWAG MCGEMAGDEI AIPILLGLGL DEFSMSATSI LPARTQIKDL
     SKKELASFKD QILSMGTAEE VVDFIKEKTQ K
//
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