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PTFX_ECOL6
ID   PTFX_ECOL6              Reviewed;         831 AA.
AC   Q8FFD8;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Multiphosphoryl transfer protein {ECO:0000250|UniProtKB:P77439};
DE            Short=MTP {ECO:0000250|UniProtKB:P77439};
DE   AltName: Full=Triphosphoryl transfer protein {ECO:0000250|UniProtKB:P77439};
DE            Short=TTP {ECO:0000250|UniProtKB:P77439};
DE   Includes:
DE     RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000250|UniProtKB:P77439};
DE              EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE     AltName: Full=Phosphotransferase system enzyme I {ECO:0000250|UniProtKB:P77439};
DE   Includes:
DE     RecName: Full=Phosphocarrier protein HPr {ECO:0000250|UniProtKB:P77439};
DE              Short=Protein H {ECO:0000250|UniProtKB:P77439};
DE   Includes:
DE     RecName: Full=PTS system fructose-like EIIA component {ECO:0000250|UniProtKB:P77439};
DE              EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE     AltName: Full=Fructose-like phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P77439};
GN   Name=fryA; OrderedLocusNames=c2922;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Multifunctional protein that includes general (non sugar-
CC       specific) and sugar-specific components of the phosphoenolpyruvate-
CC       dependent sugar phosphotransferase system (sugar PTS). This major
CC       carbohydrate active transport system catalyzes the phosphorylation of
CC       incoming sugar substrates concomitantly with their translocation across
CC       the cell membrane. The enzyme II FryABC PTS system is involved in
CC       fructose transport. {ECO:0000250|UniProtKB:P77439}.
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:0000250|UniProtKB:P08839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         fructose 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC         ChEBI:CHEBI:64837; EC=2.7.1.202;
CC         Evidence={ECO:0000250|UniProtKB:P20966};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P08839};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC   -!- DOMAIN: In contrast to classical PTS systems, the fructose-like PTS has
CC       no requirement for HPr and Enzyme I; FryA combines a IIA domain with an
CC       Enzyme I and a HPr domains. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN81372.1; -; Genomic_DNA.
DR   RefSeq; WP_000955876.1; NC_004431.1.
DR   AlphaFoldDB; Q8FFD8; -.
DR   SMR; Q8FFD8; -.
DR   STRING; 199310.c2922; -.
DR   PRIDE; Q8FFD8; -.
DR   EnsemblBacteria; AAN81372; AAN81372; c2922.
DR   KEGG; ecc:c2922; -.
DR   eggNOG; COG1080; Bacteria.
DR   eggNOG; COG1762; Bacteria.
DR   eggNOG; COG1925; Bacteria.
DR   HOGENOM; CLU_007308_5_1_6; -.
DR   OMA; EMLFMDR; -.
DR   BioCyc; ECOL199310:C2922-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 1.10.274.10; -; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   Gene3D; 3.30.1340.10; -; 1.
DR   Gene3D; 3.40.930.10; -; 1.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_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; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR006318; PTS_EI-like.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR004715; PTS_IIA_fruc.
DR   InterPro; IPR036618; PtsI_HPr-bd_sf.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF47831; SSF47831; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   SUPFAM; SSF55594; SSF55594; 1.
DR   SUPFAM; SSF55804; SSF55804; 1.
DR   TIGRFAMs; TIGR00848; fruA; 1.
DR   TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphoprotein;
KW   Phosphotransferase system; Sugar transport; Transferase; Transport.
FT   CHAIN           1..831
FT                   /note="Multiphosphoryl transfer protein"
FT                   /id="PRO_0000147098"
FT   DOMAIN          1..90
FT                   /note="HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   DOMAIN          685..828
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   REGION          119..650
FT                   /note="PTS EI"
FT                   /evidence="ECO:0000250|UniProtKB:P77439"
FT   ACT_SITE        15
FT                   /note="Pros-phosphohistidine intermediate; for HPr
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT   ACT_SITE        298
FT                   /note="Tele-phosphohistidine intermediate; for PTS EI
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08839,
FT                   ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        611
FT                   /note="Proton donor; for EI activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   ACT_SITE        747
FT                   /note="Tele-phosphohistidine intermediate; for PTS EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   BINDING         405
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
FT   BINDING         441
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         540
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         563..564
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         564
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P08839"
FT   BINDING         574
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P23533"
FT   MOD_RES         15
FT                   /note="Phosphohistidine; by EI"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         298
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         747
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   831 AA;  92079 MW;  17ED5E3F7B000090 CRC64;
     MLTIQFLCPL PNGLHARPAW ELKEQCSQWQ SEITFINHRQ NAKADAKSSL ALIGTGTLFN
     DSCSLNISGS DEEQARRVLE EYIQVRFIDS DSVQPTLAEL TAHPLPRSLS RLNPDLLYGN
     VLASGVGVGT LTLLQSDSLD SYRVIPASAQ DSTLLEHSLA TLAEQLNQQL RERDGESKTI
     LSAHLSLIQD DEFAGNIRHL MAEQHQGLGA AIISNMEQIC AKLSASASDY LRERVSDIRD
     ISEQLLHITW PELKPRNNLV LEKPTILVAE DLTPSQFLSL DLKNLAGMIL EKTGRTSHTL
     ILARASAIPV LSGLPLDAIA RYAGQPAVLD AQCGVLAINP NDAVSGYYQV AQTLADKRQK
     QQAQAAAQLA YSRDKKRIDI AANIGTALEA PGAFANGAEG VGLFRTEMLY MDRDSAPDEQ
     EQFEAYQQVL LAAGDKPIIF RTMDIGGDKS IPYLNIPQEE NPFLGYRAVR IYPEFAGLFR
     TQLRAILRAA SFGNAQLMIP MVHSLDQILW VKGELQKAIV ELKRDGLRHA ETITLGIMVE
     VPSVCYIIDH FCDEVDFFSI GSNDMTQYLY AVDRNNPRVS PLYNPITPSF LRMLQQIVTA
     AHQRGKWVGI CGELGGESRY LPLLLGLGLD ELSMSSPRIP AVKSQLRQLD SEACRELARQ
     ACECRSAQEI EALLTAFTPE EDVRPLLALE NIFVDQSFSN KEQAIQFLCG NLGVNGRTEH
     PFELEEDVWQ REEIVTTGVG FGVAIPHTKS QWIRHSSISI ARLVKPVDWQ SEMGEVELVI
     MLTLGANEGM NHVKVFSQLA RKLVNKNFRQ SLFAAQDAQS ILTLLETELT F
 
 
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