PTFBC_ECOLI
ID PTFBC_ECOLI Reviewed; 563 AA.
AC P20966;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=PTS system fructose-specific EIIB'BC component {ECO:0000305|PubMed:8626640};
DE AltName: Full=EIIB'BC-Fru {ECO:0000305|PubMed:8626640};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIB component {ECO:0000303|PubMed:3076173};
DE EC=2.7.1.202 {ECO:0000269|PubMed:8626640, ECO:0000305|PubMed:3510127};
DE AltName: Full=EIII-Fru {ECO:0000303|PubMed:3076173};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:3076173};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIC component {ECO:0000303|PubMed:3076173};
DE AltName: Full=Fructose permease IIC component {ECO:0000303|PubMed:3076173};
GN Name=fruA {ECO:0000303|PubMed:3076173}; Synonyms=ptsF;
GN OrderedLocusNames=b2167, JW2154;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, FUNCTION,
RP SUBCELLULAR LOCATION, AND ACTIVE SITE.
RC STRAIN=K12;
RX PubMed=3076173; DOI=10.1099/00221287-134-10-2757;
RA Prior T.I., Kornberg H.L.;
RT "Nucleotide sequence of fruA, the gene specifying enzyme IIfru of the
RT phosphoenolpyruvate-dependent sugar phosphotransferase system in
RT Escherichia coli K12.";
RL J. Gen. Microbiol. 134:2757-2768(1988).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-365.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
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, AND CATALYTIC ACTIVITY.
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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, DOMAIN, AND ACTIVE SITE.
RX PubMed=8626640; DOI=10.1074/jbc.271.17.9997;
RA Charbit A., Reizer J., Saier M.H. Jr.;
RT "Function of the duplicated IIB domain and oligomeric structure of the
RT fructose permease of Escherichia coli.";
RL J. Biol. Chem. 271:9997-10003(1996).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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:0000269|PubMed:8626640,
CC ECO:0000305|PubMed:3076173}.
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:0000269|PubMed:8626640, ECO:0000305|PubMed:3510127};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for fructose {ECO:0000269|PubMed:8626640};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427, ECO:0000269|PubMed:15919996,
CC ECO:0000305|PubMed:3076173}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000269|PubMed:15919996,
CC ECO:0000305|PubMed:3076173, ECO:0000305|PubMed:8626640}.
CC -!- INDUCTION: By fructose. {ECO:0000250|UniProtKB:P23355}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- DOMAIN: In the N-terminal, the PTS system fructose-specific possesses a
CC duplicated EIIB domain (EIIB' domain) which lacks the active site and
CC functions to facilitate phosphoryl transfer between the EIIA domain of
CC diphosphoryl transfer protein (DTP) and the EIIB domain. Construction
CC of a protein lacking the EIIB' domain shows that it is functional for
CC fructose transport in vivo as well as fructose phosphorylation in
CC vitro. The presence of the EIIB' domain, however, is required for
CC normal high affinity recognition of DTP by the PTS system fructose-
CC specific as well as for normal rates of phosphoryl transfer between the
CC EIIA and EIIB domains of DTP and PTS system fructose-specific,
CC respectively. {ECO:0000269|PubMed:8626640}.
CC -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M23196; AAA62624.1; -; Genomic_DNA.
DR EMBL; U00007; AAA60524.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75228.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15976.2; -; Genomic_DNA.
DR EMBL; X53948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A34962; A34962.
DR RefSeq; NP_416672.1; NC_000913.3.
DR RefSeq; WP_000854447.1; NZ_SSZK01000027.1.
DR AlphaFoldDB; P20966; -.
DR SMR; P20966; -.
DR BioGRID; 4260463; 42.
DR BioGRID; 851014; 1.
DR ComplexPortal; CPX-5941; Fructose-specific enzyme II complex.
DR IntAct; P20966; 2.
DR STRING; 511145.b2167; -.
DR TCDB; 4.A.2.1.1; the pts fructose-mannitol (fru) family.
DR jPOST; P20966; -.
DR PaxDb; P20966; -.
DR PRIDE; P20966; -.
DR EnsemblBacteria; AAC75228; AAC75228; b2167.
DR EnsemblBacteria; BAA15976; BAA15976; BAA15976.
DR GeneID; 946672; -.
DR KEGG; ecj:JW2154; -.
DR KEGG; eco:b2167; -.
DR PATRIC; fig|1411691.4.peg.72; -.
DR EchoBASE; EB0332; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR eggNOG; COG3925; Bacteria.
DR HOGENOM; CLU_013155_4_1_6; -.
DR InParanoid; P20966; -.
DR OMA; CKLMAPH; -.
DR PhylomeDB; P20966; -.
DR BioCyc; EcoCyc:FRUA-MON; -.
DR BioCyc; MetaCyc:FRUA-MON; -.
DR SABIO-RK; P20966; -.
DR PRO; PR:P20966; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IPI:ComplexPortal.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR GO; GO:0090582; F:protein-phosphocysteine-D-fructose-phosphotransferase system transporter activity; IMP:EcoCyc.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05569; PTS_IIB_fructose; 1.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 2.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing; Kinase;
KW Membrane; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Repeat; Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..563
FT /note="PTS system fructose-specific EIIB'BC component"
FT /id="PRO_0000186508"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 1..85
FT /note="PTS EIIB type-2 1"
FT /evidence="ECO:0000305|PubMed:8626640"
FT DOMAIN 104..201
FT /note="PTS EIIB type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 226..561
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT ACT_SITE 112
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000269|PubMed:8626640,
FT ECO:0000305|PubMed:3076173"
FT MOD_RES 112
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
SQ SEQUENCE 563 AA; 57519 MW; AC066A96A94DBA05 CRC64;
MKTLLIIDAN LGQARAYMAK TLLGAAARKA KLEIIDNPND AEMAIVLGDS IPNDSALNGK
NVWLGDISRA VAHPELFLSE AKGHAKPYTA PVAATAPVAA SGPKRVVAVT ACPTGVAHTF
MAAEAIETEA KKRGWWVKVE TRGSVGAGNA ITPEEVAAAD LVIVAADIEV DLAKFAGKPM
YRTSTGLALK KTAQELDKAV AEATPYEPAG KAQTATTESK KESAGAYRHL LTGVSYMLPM
VVAGGLCIAL SFAFGIEAFK EPGTLAAALM QIGGGSAFAL MVPVLAGYIA FSIADRPGLT
PGLIGGMLAV STGSGFIGGI IAGFLAGYIA KLISTQLKLP QSMEALKPIL IIPLISSLVV
GLAMIYLIGK PVAGILEGLT HWLQTMGTAN AVLLGAILGG MMCTDMGGPV NKAAYAFGVG
LLSTQTYGPM AAIMAAGMVP PLAMGLATMV ARRKFDKAQQ EGGKAALVLG LCFISEGAIP
FAARDPMRVL PCCIVGGALT GAISMAIGAK LMAPHGGLFV LLIPGAITPV LGYLVAIIAG
TLVAGLAYAF LKRPEVDAVA KAA
