ID   PTFX1_ECOLI             Reviewed;         831 AA.
AC   P77439;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 191.
DE   RecName: Full=Multiphosphoryl transfer protein 1 {ECO:0000305|PubMed:11361063};
DE            Short=MTP 1 {ECO:0000305|PubMed:11361063};
DE   AltName: Full=Triphosphoryl transfer protein 1 {ECO:0000305|PubMed:11361063};
DE            Short=TTP 1 {ECO:0000305|PubMed:11361063};
DE   Includes:
DE     RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000303|PubMed:11361063};
DE              EC=2.7.3.9 {ECO:0000250|UniProtKB:P08839};
DE     AltName: Full=Phosphotransferase system enzyme I {ECO:0000303|PubMed:11361063};
DE   Includes:
DE     RecName: Full=Phosphocarrier protein HPr {ECO:0000303|PubMed:11361063};
DE              Short=Protein H {ECO:0000303|PubMed:11361063};
DE   Includes:
DE     RecName: Full=PTS system fructose-like EIIA component {ECO:0000303|PubMed:11361063};
DE              EC=2.7.1.202 {ECO:0000250|UniProtKB:P20966};
DE     AltName: Full=Fructose-like phosphotransferase enzyme IIA component {ECO:0000303|PubMed:11361063};
GN   Name=fryA; Synonyms=ypdD; OrderedLocusNames=b2383, JW2380;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, AND DISCUSSION OF SEQUENCE.
RX   PubMed=11361063;
RA   Tchieu J.H., Norris V., Edwards J.S., Saier M.H. Jr.;
RT   "The complete phosphotransferase system in Escherichia coli.";
RL   J. Mol. Microbiol. Biotechnol. 3:329-346(2001).
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:0000305|PubMed:11361063}.
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   -!- INTERACTION:
CC       P77439; P0AFG8: aceE; NbExp=2; IntAct=EBI-545399, EBI-542683;
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; U00096; AAC75442.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16253.1; -; Genomic_DNA.
DR   PIR; D65012; D65012.
DR   RefSeq; NP_416884.1; NC_000913.3.
DR   RefSeq; WP_000955906.1; NZ_CP009789.1.
DR   AlphaFoldDB; P77439; -.
DR   SMR; P77439; -.
DR   BioGRID; 4261077; 13.
DR   DIP; DIP-12817N; -.
DR   FunCoup; P77439; 215.
DR   IntAct; P77439; 1.
DR   STRING; 511145.b2383; -.
DR   TCDB; 4.A.2.1.11; the pts fructose-mannitol (fru) family.
DR   jPOST; P77439; -.
DR   PaxDb; 511145-b2383; -.
DR   EnsemblBacteria; AAC75442; AAC75442; b2383.
DR   GeneID; 946852; -.
DR   KEGG; ecj:JW2380; -.
DR   KEGG; eco:b2383; -.
DR   KEGG; ecoc:C3026_13250; -.
DR   PATRIC; fig|1411691.4.peg.4345; -.
DR   EchoBASE; EB3903; -.
DR   eggNOG; COG1080; Bacteria.
DR   eggNOG; COG1762; Bacteria.
DR   eggNOG; COG1925; Bacteria.
DR   HOGENOM; CLU_007308_5_1_6; -.
DR   InParanoid; P77439; -.
DR   OMA; EMLFMDR; -.
DR   OrthoDB; 9765468at2; -.
DR   PhylomeDB; P77439; -.
DR   BioCyc; EcoCyc:G7246-MONOMER; -.
DR   PRO; PR:P77439; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; ISS:UniProtKB.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-carbohydrate phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0015764; P:N-acetylglucosamine transport; IBA:GO_Central.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 3.30.1340.10; HPr-like; 1.
DR   Gene3D; 3.40.930.10; Mannitol-specific EII, Chain A; 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; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR050499; PEP-utilizing_PTS_enzyme.
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   NCBIfam; TIGR00848; fruA; 1.
DR   NCBIfam; TIGR01417; PTS_I_fam; 1.
DR   PANTHER; PTHR46244:SF4; MULTIPHOSPHORYL TRANSFER PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
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   PRINTS; PR01736; PHPHTRNFRASE.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF55594; HPr-like; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transport.
FT   CHAIN           1..831
FT                   /note="Multiphosphoryl transfer protein 1"
FT                   /id="PRO_0000147097"
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:0000305|PubMed:11361063"
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;  92130 MW;  B9F3E3B6D4EAB597 CRC64;
     MLTIQFLCPL PNGLHARPAW ELKEQCSQWQ SEITFINHRQ NAKADAKSSL ALIGTGTLFN
     DSCSLNISGS DEEQARRVLE EYIQVRFIDS DSVQPTQAEL TAHPLPRSLS RLNPDLLYGN
     VLASGVGVGT LTLLQSDSLD SYRAIPASAQ DSTRLEHSLA TLAEQLNQQL RERDGESKTI
     LSAHLSLIQD DEFAGNIRRL MTEQHQGLGA AIISNMEQVC AKLSASASDY LRERVSDIRD
     ISEQLLHITW PELKPRNKLV LEKPTILVAE DLTPSQFLSL DLKNLAGMIL EKTGRTSHTL
     ILARASAIPV LSGLPLDAIA RYAGQPAVLD AQCGVLAINP NDAVSGYYQV AQTLADKRQK
     QQAQAAAQLA YSRDNKRIDI AANIGTALEA PGAFANGAEG VGLFRTEMLY MDRDSAPDEQ
     EQFEAYQQVL LAAGDKPIIF RTMDIGGDKS IPYLNIPQEE NPFLGYRAVR IYPEFAGLFR
     TQLRAILRAA SFGNAQLMIP MVHSLDQILW VKGEIQKAIV ELKRDGLRHA ETITLGIMVE
     VPSVCYIIDH FCDEVDFFSI GSNDMTQYLY AVDRNNPRVS PLYNPITPSF LRMLQQIVTT
     AHQRGKWVGI CGELGGESRY LPLLLGLGLD ELSMSSPRIP AVKSQLRQLD SEACRELARQ
     ACECRSAQEI EALLTAFTPE EDVRPLLALE NIFVDQDFSN KEQAIQFLCG NLGVNGRTEH
     PFELEEDVWQ REEIVTTGVG FGVAIPHTKS QWIRHSSISI ARLAKPIGWQ SEMGEVELVI
     MLTLGANEGM NHVKVFSQLA RKLVNKNFRQ SLFAAQDAQS ILTLLETELT F
//