PTFAH_ECOLI
ID PTFAH_ECOLI Reviewed; 376 AA.
AC P69811; P24217; P94759;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Multiphosphoryl transfer protein {ECO:0000250|UniProtKB:P44715};
DE Short=MTP {ECO:0000250|UniProtKB:P44715};
DE AltName: Full=Diphosphoryl transfer protein {ECO:0000303|PubMed:8013873};
DE Short=DTP {ECO:0000303|PubMed:8013873};
DE AltName: Full=Phosphotransferase FPr protein {ECO:0000250|UniProtKB:P17127};
DE AltName: Full=Pseudo-HPr {ECO:0000250|UniProtKB:P17127};
DE Includes:
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000250|UniProtKB:P17127};
DE Short=Protein H {ECO:0000250|UniProtKB:P17127};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000303|PubMed:8013873};
DE AltName: Full=EIIA-Fru {ECO:0000250|UniProtKB:P17127};
DE AltName: Full=EIII-Fru {ECO:0000250|UniProtKB:P17127};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:8013873};
GN Name=fruB {ECO:0000303|PubMed:8013873}; Synonyms=fpr, fruF;
GN OrderedLocusNames=b2169, JW2156;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION, AND FUNCTION.
RX PubMed=8013873; DOI=10.1111/j.1574-6968.1994.tb06819.x;
RA Reizer J., Reizer A., Kornberg H.L., Saier M.H. Jr.;
RT "Sequence of the fruB gene of Escherichia coli encoding the diphosphoryl
RT transfer protein (DTP) of the phosphoenolpyruvate: sugar phosphotransferase
RT system.";
RL FEMS Microbiol. Lett. 118:159-162(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 59.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 274-376.
RC STRAIN=K12;
RX PubMed=1981619; DOI=10.1098/rspb.1990.0108;
RA Orchard L.M.D., Kornberg H.L.;
RT "Sequence similarities between the gene specifying 1-phosphofructokinase
RT (fruK), genes specifying other kinases in Escherichia coli K12, and lacC of
RT Staphylococcus aureus.";
RL Proc. R. Soc. B 242:87-90(1990).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN STRUCTURE.
RX PubMed=3510127; DOI=10.1016/0014-5793(86)80042-4;
RA Kornberg H.;
RT "The roles of HPr and FPr in the utilization of fructose by Escherichia
RT coli.";
RL FEBS Lett. 194:12-15(1986).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II FruAB PTS system is involved in fructose transport.
CC {ECO:0000269|PubMed:3510127, ECO:0000305|PubMed:8013873}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by fructose and repressed by FruR.
CC {ECO:0000250|UniProtKB:P17127}.
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-specific PTS
CC has no requirement for HPr; FruB combines a IIA domain with a HPr
CC domain. {ECO:0000305|PubMed:3510127}.
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DR EMBL; S72443; AAB31084.1; -; Genomic_DNA.
DR EMBL; U00007; AAA60534.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75230.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15978.2; -; Genomic_DNA.
DR EMBL; X53948; CAA37895.1; -; Genomic_DNA.
DR PIR; I53564; I53564.
DR RefSeq; NP_416674.1; NC_000913.3.
DR RefSeq; WP_000487246.1; NZ_SSZK01000027.1.
DR AlphaFoldDB; P69811; -.
DR SMR; P69811; -.
DR BioGRID; 4260464; 19.
DR BioGRID; 851019; 2.
DR ComplexPortal; CPX-5941; Fructose-specific enzyme II complex.
DR DIP; DIP-48096N; -.
DR IntAct; P69811; 7.
DR STRING; 511145.b2169; -.
DR TCDB; 4.A.2.1.1; the pts fructose-mannitol (fru) family.
DR SWISS-2DPAGE; P69811; -.
DR jPOST; P69811; -.
DR PaxDb; P69811; -.
DR PRIDE; P69811; -.
DR EnsemblBacteria; AAC75230; AAC75230; b2169.
DR EnsemblBacteria; BAA15978; BAA15978; BAA15978.
DR GeneID; 946677; -.
DR KEGG; ecj:JW2156; -.
DR KEGG; eco:b2169; -.
DR PATRIC; fig|1411691.4.peg.70; -.
DR EchoBASE; EB0005; -.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_046384_0_0_6; -.
DR OMA; QGIEWGE; -.
DR PhylomeDB; P69811; -.
DR BioCyc; EcoCyc:FRUB-MON; -.
DR BioCyc; MetaCyc:FRUB-MON; -.
DR PRO; PR:P69811; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1902495; C:transmembrane transporter complex; IPI:ComplexPortal.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:1990539; P:fructose import across plasma membrane; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
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; 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; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR Pfam; PF00381; PTS-HPr; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF55594; SSF55594; 1.
DR SUPFAM; SSF55804; SSF55804; 2.
DR TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
DR PROSITE; PS00589; PTS_HPR_SER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..376
FT /note="Multiphosphoryl transfer protein"
FT /id="PRO_0000186516"
FT DOMAIN 2..142
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT DOMAIN 285..375
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT REGION 156..284
FT /note="M domain"
FT /evidence="ECO:0000250|UniProtKB:P44715"
FT ACT_SITE 62
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 299
FT /note="Pros-phosphohistidine intermediate; for HPr
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT MOD_RES 62
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
FT MOD_RES 299
FT /note="Phosphohistidine; by EI"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> T (in Ref. 3; BAA15978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 39648 MW; D4D953E69E2090FF CRC64;
MFQLSVQDIH PGEKAGDKEE AIRQVAAALV QAGNVAEGYV NGMLAREQQT STFLGNGIAI
PHGTTDTRDQ VLKTGVQVFQ FPEGVTWGDG QVAYVAIGIA ASSDEHLGLL RQLTHVLSDD
SVAEQLKSAT TAEELRALLM GEKQSEQLKL DNEMLTLDIV ASDLLTLQAL NAARLKEAGA
VDATFVTKAI NEQPLNLGQG IWLSDSAEGN LRSAIAVSRA ANAFDVDGET AAMLVSVAMN
DDQPIAVLKR LADLLLDNKA DRLLKADAAT LLALLTSDDA PTDDVLSAEF VVRNEHGLHA
RPGTMLVNTI KQFNSDITVT NLDGTGKPAN GRSLMKVVAL GVKKGHRLRF TAQGADAEQA
LKAIGDAIAA GLGEGA
