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Database: UniProt
Entry: A0A099P9T3_9GAMM
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ID   A0A099P9T3_9GAMM        Unreviewed;       767 AA.
AC   A0A099P9T3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=LH51_17920 {ECO:0000313|EMBL:KGK40974.1};
OS   Nitrincola sp. A-D6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK40974.1, ECO:0000313|Proteomes:UP000029924};
RN   [1] {ECO:0000313|EMBL:KGK40974.1, ECO:0000313|Proteomes:UP000029924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-D6 {ECO:0000313|EMBL:KGK40974.1,
RC   ECO:0000313|Proteomes:UP000029924};
RA   Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA   Fernandez S., Ferrer A., Chavez R., Levican G.;
RT   "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT   Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:KGK40974.1}.
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DR   EMBL; JRLB01000110; KGK40974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099P9T3; -.
DR   STRING; 1545442.LH51_17920; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000029924; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:KGK40974.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029924};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGK40974.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          17..164
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
FT   COILED          212..239
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   767 AA;  84631 MW;  6A5167DFD6758928 CRC64;
     MLKVLRQIVQ DVSTAPDLNA VLQITVGRVQ KAMKTEVCSV FLFNQESGRY VLRATKGLNA
     AAVDEVSLAK DEGIVGLVAK RAEPINLEDA SSHPAFHYLD VTGEELFHAF LGVPIMHQRK
     VLGVLVVQQQ ERRRFDESEE AFLVTLSAQL AGIIAHAHAT GAIQMAGEKG VAKQLRNDLR
     YDGVAAAGGV VIGEIVVASL PSDLDSVPDK QSDDVALELE QLEQALIAVR KEIGLVAENL
     AGRLSKDERA LFDVYLRMLD DNGLPMEMRA KIQQGSWAQG ALREVILEHV RAFSAMDDPY
     LSERATDIKD LGKRILQHLQ EDNNGRNLEY PENAVLLADE LTPAMLGLVP EGKLSGLISI
     TGSGNSHAAI LARSMGIPTV MGVVDLPYRR LNGAAVIVDG YSGRIYINPS IELVQAFSRI
     VVDEKVVEDE LRVLRDLPAI TKDGYRLPLW VNTGLAADVP RSLEQGAEGI GLYRTEIPFM
     IRDSFPSEQE QLESYRTQLQ AFAPMPVTMR TLDIGGDKAL PYFPIKEENP SLGWRGIRVT
     LDHPEIFMVQ VRAMLRASEG LNNLRIMLPM VTSVSEVDEA LRQIDRACEE LREEGYHINK
     PPVGVMIEVP AAVYQTRRFA RLVDFISVGS NDLTQYLLAV DRNNPRVAGL YASYHPAVLK
     ALDFIVHEAH KERKHVSICG EIAADPGGAL LLMAMGYDVL SVNANNLPKI KFAIRSVSFA
     RARQLLLSVR SLHDAEEIHQ ELRQSLKAFG LTRLTRPLMP DQKTPSC
//
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