ID A0A285JXW9_9ENTR Unreviewed; 748 AA.
AC A0A285JXW9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=SAMN02744775_01185 {ECO:0000313|EMBL:SNY64903.1};
OS Enterobacter sp. CC120223-11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=1378073 {ECO:0000313|EMBL:SNY64903.1, ECO:0000313|Proteomes:UP000219512};
RN [1] {ECO:0000313|EMBL:SNY64903.1, ECO:0000313|Proteomes:UP000219512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC120223-11 {ECO:0000313|EMBL:SNY64903.1,
RC ECO:0000313|Proteomes:UP000219512};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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; OBEF01000004; SNY64903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285JXW9; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000219512; 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; IPR018274; PEP_util_AS.
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.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 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 Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..164
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 748 AA; 83462 MW; 6E9467D086FF96A5 CRC64;
MLTRLREIVE KVASAPRVNE ALDILVTDIC QAMETEVCSV YLADHDRRCY YLMATRGLKK
PRGRTITLAF DEGVVGLVGR LAEPINLADA QKHPSFKYIP SVKEEKYRAF LGVPIIQRRQ
LLGVLVVQQR ELRQYDESEE SFLVTLATQM AAILSQSQLT ALFGQYRQTR IRALPASSGV
AIAQGWMDAT LPLMEQVYEA STLDTVLERE RLTGALEEAA GEFRRYSKRF AAGAQKETAA
IFDLYSHLLS DARLRKELFA EVDKGSVAEW AVKTIIEKFA AQFAALSDGY LKERAGDLRA
LGQRLLFHLD DTVQGANAWP ERFVLVADEL SATTLAEVPQ DRLTGVVVRD GAANSHAAIM
VRALGIPTVM GADIQPSVLH GRMLVVDGYR GELLVDPEPV LLQEYQRLVT EENELSRIAE
DDVERPAQLK TGERVKVMLN AGLSPEHEEK LGSRIDGIGL YRTEIPFMLQ SGFPSEEEQV
AQYQGMLQMF NDKPVTLRTL DVGADKQLPY MPISEENPCL GWRGIRITLD QPEIFLVQVR
AMLRANAATG NLSILLPMVT SIDEVDEAKR LIERAGREVE EMIGYEIPKP RIGVMLEVPS
MVFLMPHLVN RVDFISVGTN DLTQYLLAVD RNNTRVASIY DSLHPALLRA LSMIAQESER
HGLDLRLCGE MAGDPMCVTI LIGLGFRHLS MNGRSVARVK YLLRNIELEE AQNLAQRSLE
AQLATEVRHQ VAAFMERRGL GGLIRGGR
//