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Database: UniProt
Entry: G4FBP1_9GAMM
LinkDB: G4FBP1_9GAMM
Original site: G4FBP1_9GAMM 
ID   G4FBP1_9GAMM            Unreviewed;       753 AA.
AC   G4FBP1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=HAL1_19136 {ECO:0000313|EMBL:EHA13908.1};
OS   Halomonas sp. HAL1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA13908.1, ECO:0000313|Proteomes:UP000005692};
RN   [1] {ECO:0000313|EMBL:EHA13908.1, ECO:0000313|Proteomes:UP000005692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX   PubMed=22156396; DOI=10.1128/JB.06359-11;
RA   Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA   Wang G., Rensing C.;
RT   "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT   Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL   J. Bacteriol. 194:199-200(2012).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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:EHA13908.1}.
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DR   EMBL; AGIB01000087; EHA13908.1; -; Genomic_DNA.
DR   RefSeq; WP_008959682.1; NZ_CP130610.1.
DR   AlphaFoldDB; G4FBP1; -.
DR   PATRIC; fig|550984.5.peg.3710; -.
DR   Proteomes; UP000005692; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
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; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
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:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PRINTS; PR01736; PHPHTRNFRASE.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Pyruvate {ECO:0000313|EMBL:EHA13908.1};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHA13908.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          17..164
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   753 AA;  82913 MW;  D7D5B8CDB05A8475 CRC64;
     MLEVLRRVIQ EVNGARNLDA ALSTMVRRIR KAMQTDVCSF YLYDKELESL VLMETIGLRT
     QAVGRVVLPL GEGLVGLVAK RSEPLNLEDA QAHPQFRYFE ATGEERYSSF LGVPIIHQRH
     MLGVLVVQQA EKRRYDDEDE AFLVTMAAQL AGVLAHALAT GNLMRPALAG GQAMFKGVAA
     SPGMAMGEAV VITPPADLNS VPDLVPSDLD YEVARLKEAI GKTRSEIRAA AERLASRISA
     QELALFDVYQ QMLGEAALAD EVEKRIREGQ WAPGALADVV RRHVQYLERV DDNYLRERAA
     DIRDLGRRVL AHLQEDTPST PETYPDNAIL VGDEISVAML GEVPRDKLKG LVSVRGSSTS
     HVAIVARAMG IPTVLGMVDL PLPRLGGAPV VLDGHRGRLF VRPAPELKAR YASLIAEEEA
     LSELLEHEQD LPSATPDGHI MPLMVNTGLA VDATALLKSR IGGVGLYRTE VPFMITERFP
     GEKEQTRLYR DQLEGFAPLP VVMRTLDIGG DKDLPYFPIE EANPFLGWRG MRVTLDHPEV
     LMVQLRAMLK ASIDLDNLYV LFPMITNVEE VDEALRLLDR AILELGEEGI TVIRPQVGVM
     IEVPATIYQM DALAKRVDFF SVGSNDLTQY LLAVDRNNPR VSSLYDALHP ALLGALLELA
     NDATRLNKPI SLCGELAGDP AGALLLMAMG FTSLSMNAPS LPKVRAAIRR VPFSDAQQLL
     KEVMELDTPA QVHAHLDQRL DEWQLSHLMP PRD
//
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