Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

phosphoenolpyruvate--protein phosphotransferase [Escherichia coli].


LOCUS       WP_001174066             833 aa            linear   BCT 17-JUN-2024
ACCESSION   WP_001174066
VERSION     WP_001174066.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01417.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..833
                     /gene="ptsP"
     Protein         1..833
                     /product="phosphoenolpyruvate--protein phosphotransferase"
                     /EC_number="2.7.3.9"
                     /GO_function="GO:0008965 - phosphoenolpyruvate-protein
                     phosphotransferase activity [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=91691
     Region          6..84
                     /region_name="PTS-HPr_like"
                     /note="Histidine-containing phosphocarrier protein
                     (HPr)-like proteins. HPr is a central component of the
                     bacterial phosphoenolpyruvate sugar phosphotransferase
                     system (PTS). The PTS catalyses the phosphorylation of
                     sugar substrates during their translocation...; cd00367"
                     /db_xref="CDD:238217"
     Site            6..9
                     /site_type="other"
                     /note="dimerization domain swap beta strand [polypeptide
                     binding]"
                     /db_xref="CDD:238217"
     Site            order(15,17..18,20..21,25,28,48..51,54..55)
                     /site_type="other"
                     /note="regulatory protein interface [polypeptide binding]"
                     /db_xref="CDD:238217"
     Site            16
                     /site_type="active"
                     /db_xref="CDD:238217"
     Site            49
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238217"
     Region          123..684
                     /region_name="PtsA"
                     /note="Phosphoenolpyruvate-protein kinase (PTS system EI
                     component in bacteria) [Carbohydrate transport and
                     metabolism]; COG1080"
                     /db_xref="CDD:440698"
     Region          687..831
                     /region_name="PtsN"
                     /note="Phosphotransferase system
                     mannitol/fructose-specific IIA domain (Ntr-type)
                     [Carbohydrate transport and metabolism, Signal
                     transduction mechanisms]; COG1762"
                     /db_xref="CDD:441368"
ORIGIN      
        1 malivefice lpngvharpa shvetlcntf ssqiewhnlr tdrkgnaksa laligtdtla
       61 gdncqllisg adeqeahqrl sqwlrdefph cdaplaevks deleplpvsl tnlnpqiira
      121 rtvcsgsagg iltpissldl nalgnlpaak dvdaeqsale ngltlvlkni efrlldsdga
      181 tsaileahrs lagdtslheh llagvsagls caeaivasan hfceefsrss ssylqerald
      241 vrdvcfqllq qiygeqrfpa pgkltqpaic madeltpsqf leldknhlkg lllksggtts
      301 htvilarsfn iptlvgvdid altpwqhqti yidgnagaiv vepgeavary yqqearvqda
      361 lreqqrvwlt qqartadgir ieiaaniahs veaqaafgng aegvglfrte mlymdrtsap
      421 geselynifc qalesangrs iivrtmdigg dkpvdylnip aeanpflgyr avriyeeyas
      481 lfttqlrsil rasahgslki mipmissmee ilwvkeklae akqqlrnehi pfdekiqlgi
      541 mlevpsvmfi idqcceeidf fsigsndltq yllavdrdna kvtrhynsln paflraldya
      601 vqavhrqgkw iglcgelgak gsvlpllvgl gldelsmsap sipaakarma qldsrecrkl
      661 lnqamacrts levehllaqf rmtqqdaplv taecitlesd wrskeevlkg mtdnlllagr
      721 cryprklead lwareavfst glgfsfaiph sksehieqst isvarlqapv rwgddeaqfi
      781 imltlnkhaa gdqhmrifsr larrimheef rnalvnaasa daiasllqhe lel