ID A0A1U9NDR1_9GAMM Unreviewed; 755 AA.
AC A0A1U9NDR1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=B0D95_16855 {ECO:0000313|EMBL:AQT61594.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT61594.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT61594.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT61594.1,
RC ECO:0000313|Proteomes:UP000189646};
RA Peterson S.W.;
RL Submitted (FEB-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; CP019799; AQT61594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9NDR1; -.
DR STRING; 1945512.B0D95_16855; -.
DR KEGG; ceb:B0D95_16855; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000189646; Chromosome.
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:AQT61594.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189646};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AQT61594.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..163
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 755 AA; 83448 MW; 4DA9BC88AFA392E4 CRC64;
MLNSLRSIVQ EVNAARDMKS ALAIIVSRVK EVMKTQVCSV YLRDSKGDYV LMATDGLNAN
SVGKVRLAAG EGLVGRVVVR EEPINLEHAE AHPSYQYFPE TGEERYSSFL GVPIIHHRKV
LGVLVVQQVE QRRFDEGEEA FLVTMSAQLA GVIAHAEATG GVVPPGAKAS QAKFLGVSGA
SGIAIGEAVV LTPTADLRSV PYQACKDVEA EIAFFQRSLL AVREDIKSLG EQLRARINRE
EQALFDAYLA MLDDASLARE VMDRIRKGAS APYAWSEVIL EHETIFNSMN DPYLRERATD
VRDLGRRVLA YLQESNQKAR VYPDKTILIG EELTASMLGE IPKEKLAGLV SVLGSSNSHV
AILARAMDIP TVMGAVDLPY SQINGRPIIV DGYKGAVYCD PNAQLRKHYK AIYLEEQALV
KGLEALKNLP CETQDRYRLP LHVNTGLMAD VVRSLERGAE GVGLYRTEVP FLLRDRFPSE
EEQRAIYREQ LEAFAPHSVT MRTLDIGGDK ALPYFPIQED NPFLGWRGIR VTLDHPEIFL
AQIRAMIKAS EGLDNLRILL PMITNMQEVD ASRALIRRVY KELLEEGFKV RLPQVGVMIE
VPAAVYLAPE LSRRVDFLSV GSNDLTQYLL AVDRNNAQVA DLYQAFHPAV LRALQYIVYA
AHDAGISVSI CGELAGDPGA AILLMAMGFD VLSMNATNLP KVKSVIRGIT FDRAKQLLAE
VMSMSNGDQI RDHIARELRD TGLTRLIRPV TSDSN
//
