ID A0A1Y6CB22_9ALTE Unreviewed; 754 AA.
AC A0A1Y6CB22;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=SAMN02745866_03528 {ECO:0000313|EMBL:SMF55054.1};
OS Alteromonadaceae bacterium Bs31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae.
OX NCBI_TaxID=1304903 {ECO:0000313|EMBL:SMF55054.1, ECO:0000313|Proteomes:UP000192901};
RN [1] {ECO:0000313|EMBL:SMF55054.1, ECO:0000313|Proteomes:UP000192901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bs31 {ECO:0000313|EMBL:SMF55054.1,
RC ECO:0000313|Proteomes:UP000192901};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FXAI01000010; SMF55054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6CB22; -.
DR STRING; 1304903.SAMN02745866_03528; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000192901; 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 Reference proteome {ECO:0000313|Proteomes:UP000192901};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SMF55054.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..163
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT COILED 204..242
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 754 AA; 83441 MW; 5491A9343DD506CF CRC64;
MLNSLRSIVQ EVNAAADLNA VLEIIVSRVR QAMSTEVCSV YLRSANDNFM LMATEGLNQQ
AVGEVKLSLN EGLVGYVAFR EEPLNLDDAE SHPKYQYFAA TGEERFRSFL GVPIIHHRQI
LGVLVVQQRE KRRFDEGEEA FLVTMSAQLA AVIAHAEATG ALRTIGPKTE VRFMGVPGAS
GVAIGEAVVV APLADLKSVP YQTCDNVEEE LAFFQEGLAA VREDIKKLAS QLESRLNREE
RILFDAYIGM LDDTALGGEV TEKIRGGLAA PSAWSEVILE HVKIFSSMHD PYLQERASDV
RDLGSRVLAY LQESAKREQQ PAYPENTILV GEDLTASVLA EVPEGRLVGI VSTRGSSNSH
IAILARSIGI PTVMGAVDLP FTRMEGRELI VDGYRGSVYS DPSESLRVQY QAIVEEDVQL
VAGLEALKDL PCETLDHHRV ALWVNTGLMA DAMISLERGA EGVGLYRTEI PFMLRDRFPS
EEEQRQTYRD QLAAFAPHTV TMRTLDVGGD KSLPYFPIEE ENPFLGWRGI RVTLDHPEIF
LVQIRAMLKA SEGLDNLRIM LPMVSNISEL EIAQMLLYRA YDELLEEGHK VKMPPLGVMI
EVPGAVYQTK DFAARVDFLS VGSNDLTQYL LAVDRNNPRV ADLYHSMHPA VLRALYHVVK
DSHSQGVPVS ICGEVAGDPA AALLLMAMGY DVLSMSATHL LKVKSVVRSI SLQQAEELLA
EVMVLPDTES IHRCIDATFR QFGLTRIVRP MREE
//
