PTFX1_ECOLI
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 03-AUG-2022, entry version 178.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_LN832404.1.
DR AlphaFoldDB; P77439; -.
DR SMR; P77439; -.
DR BioGRID; 4261077; 13.
DR DIP; DIP-12817N; -.
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; P77439; -.
DR PRIDE; P77439; -.
DR EnsemblBacteria; AAC75442; AAC75442; b2383.
DR EnsemblBacteria; BAA16253; BAA16253; BAA16253.
DR GeneID; 946852; -.
DR KEGG; ecj:JW2380; -.
DR KEGG; eco:b2383; -.
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 PhylomeDB; P77439; -.
DR BioCyc; EcoCyc:G7246-MON; -.
DR PRO; PR:P77439; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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 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
