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Database: UniProt
Entry: L0KEC5_HALHC
LinkDB: L0KEC5_HALHC
Original site: L0KEC5_HALHC 
ID   L0KEC5_HALHC            Unreviewed;       569 AA.
AC   L0KEC5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
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   OrderedLocusNames=Halha_2539 {ECO:0000313|EMBL:AGB42413.1};
OS   Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Halobacteroides.
OX   NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB42413.1, ECO:0000313|Proteomes:UP000010880};
RN   [1] {ECO:0000313|Proteomes:UP000010880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC   {ECO:0000313|Proteomes:UP000010880};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Halobacteroides halobius DSM 5150.";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; CP003359; AGB42413.1; -; Genomic_DNA.
DR   RefSeq; WP_015328126.1; NC_019978.1.
DR   AlphaFoldDB; L0KEC5; -.
DR   STRING; 748449.Halha_2539; -.
DR   KEGG; hhl:Halha_2539; -.
DR   PATRIC; fig|748449.3.peg.2461; -.
DR   eggNOG; COG1080; Bacteria.
DR   HOGENOM; CLU_007308_7_0_9; -.
DR   OMA; CNAEWAL; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000010880; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:AGB42413.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010880};
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..127
FT                   /note="Phosphotransferase system enzyme I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05524"
FT   DOMAIN          153..226
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          252..540
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   COILED          34..107
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        190
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         297
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   569 AA;  63286 MW;  B2A3A5BA0B3645B4 CRC64;
     MSQQLTGVAA SPGIVTGEVM LLEEEDLSYE TVNVEDTDGE KERLHDAIQE SKEQLQAIKD
     KVEDDMGQDK AEIFQAHLMV VEDPELISAV EDKIDSEEIN VEAALEQTVE QFATMFSNMD
     DEYMRERASD IRDVGTRILR NLLGVENMSL AELDREVILV AEDLTPSDTA QVDKDKVLGF
     ATKVGGRTSH TAIMARSLEI PAVVGASQIL DKVENGMEII VDGVNGDVII EPTADELTNY
     QKKAQEYRER RKRLAQLKEE PAETKDGHQV ELVANIGTPN DVAGALDKGA EGIGLYRSEF
     LYMDRDSLPT EKEQFEAYKE VAEKMDGPIV IRTLDIGGDK ELSYLDLPEE MNPFLGYRAI
     RICLDKTDIF KTQLRAILKA SAYGQVKIMY PMISAVEQLR AANQILEEVK SDLSKEGIEF
     DQDLEVGMMI EVPAAAMTAD ILAKETDFFS IGTNDLIQYT TATDRMNENI AHLYQPFHPA
     LLRLIKRVVK AAHNEGNWAG MCGEMAGDKR LTPFLLGIGL DEFSMSAVTI PEVKDAIRNL
     TLEEAEKIAD EAIGYSTAEE IENYLSQQV
//
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