FABR_ECOLI
ID FABR_ECOLI Reviewed; 234 AA.
AC P0ACU5; P27307; Q2M8Q8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=HTH-type transcriptional repressor FabR {ECO:0000303|PubMed:11160901};
GN Name=fabR {ECO:0000303|PubMed:11160901}; Synonyms=yijC;
GN OrderedLocusNames=b3963, JW3935;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110;
RX PubMed=1447162; DOI=10.1128/jb.174.23.7878-7879.1992;
RA Gustafsson C., Warne S.R.;
RT "Physical map of the oxyR-trmA region (minute 89.3) of the Escherichia coli
RT chromosome.";
RL J. Bacteriol. 174:7878-7879(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN REGULATION OF FATTY ACID
RP BIOSYNTHESIS, AND DNA-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11160901; DOI=10.1093/nar/29.3.774;
RA McCue L.A., Thompson W., Carmack C.S., Ryan M.P., Liu J.S., Derbyshire V.,
RA Lawrence C.E.;
RT "Phylogenetic footprinting of transcription factor binding sites in
RT proteobacterial genomes.";
RL Nucleic Acids Res. 29:774-782(2001).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11859088; DOI=10.1074/jbc.m201399200;
RA Zhang Y.-M., Marrakchi H., Rock C.O.;
RT "The FabR (YijC) transcription factor regulates unsaturated fatty acid
RT biosynthesis in Escherichia coli.";
RL J. Biol. Chem. 277:15558-15565(2002).
RN [7]
RP FUNCTION, POSSIBLE ACTIVITY REGULATION, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP DNA-BINDING.
RC STRAIN=K12;
RX PubMed=19854834; DOI=10.1074/jbc.m109.068239;
RA Zhu K., Zhang Y.M., Rock C.O.;
RT "Transcriptional regulation of membrane lipid homeostasis in Escherichia
RT coli.";
RL J. Biol. Chem. 284:34880-34888(2009).
RN [8]
RP FUNCTION, POSSIBLE ACTIVITY REGULATION, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP DNA-BINDING.
RC STRAIN=K12;
RX PubMed=21276098; DOI=10.1111/j.1365-2958.2011.07564.x;
RA Feng Y., Cronan J.E.;
RT "Complex binding of the FabR repressor of bacterial unsaturated fatty acid
RT biosynthesis to its cognate promoters.";
RL Mol. Microbiol. 80:195-218(2011).
CC -!- FUNCTION: Binds the promoter region of at least fabA and fabB, but
CC probably not yqfA (PubMed:11160901, PubMed:19854834, PubMed:21276098).
CC Represses the transcription of fabA and fabB, involved in unsaturated
CC fatty acid (UFA) biosynthesis (PubMed:11859088). By controlling UFA
CC production, FabR directly influences the physical properties of the
CC membrane bilayer. {ECO:0000269|PubMed:11160901,
CC ECO:0000269|PubMed:11859088, ECO:0000269|PubMed:19854834,
CC ECO:0000269|PubMed:21276098}.
CC -!- ACTIVITY REGULATION: Has been suggested to require either an
CC unsaturated acyl carrier protein or unsaturated acyl-CoA (but not their
CC saturated equivalents) for DNA-binding (PubMed:19854834). Another group
CC suggests that unsaturated thioesters are not essential but act instead
CC to enhance DNA-binding (PubMed:21276098). {ECO:0000269|PubMed:19854834,
CC ECO:0000269|PubMed:21276098}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:19854834,
CC ECO:0000305|PubMed:21276098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Significantly increased levels of unsaturated
CC fatty acids (UFA) (PubMed:11859088, PubMed:19854834). Double fadR-fabR
CC deletions have increased levels of saturated fatty acids, suggesting a
CC functional fadR gene is required for fabR function (PubMed:11859088).
CC Increased transcription of fabA and fabB (PubMed:11859088,
CC PubMed:21276098). {ECO:0000269|PubMed:11859088,
CC ECO:0000269|PubMed:19854834, ECO:0000269|PubMed:21276098}.
CC -!- MISCELLANEOUS: Probably part of the fabR-yijD operon.
CC {ECO:0000305|PubMed:19854834}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-20 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC76945.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X66026; CAA46823.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43069.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76945.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP009048; BAE77348.1; -; Genomic_DNA.
DR RefSeq; NP_418398.2; NC_000913.3.
DR AlphaFoldDB; P0ACU5; -.
DR SMR; P0ACU5; -.
DR BioGRID; 4261883; 156.
DR DIP; DIP-12520N; -.
DR STRING; 511145.b3963; -.
DR PaxDb; P0ACU5; -.
DR PRIDE; P0ACU5; -.
DR EnsemblBacteria; AAC76945; AAC76945; b3963.
DR EnsemblBacteria; BAE77348; BAE77348; BAE77348.
DR GeneID; 948460; -.
DR KEGG; ecj:JW3935; -.
DR KEGG; eco:b3963; -.
DR PATRIC; fig|1411691.4.peg.2741; -.
DR EchoBASE; EB1367; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_081861_0_0_6; -.
DR InParanoid; P0ACU5; -.
DR BioCyc; EcoCyc:EG11394-MON; -.
DR PRO; PR:P0ACU5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR HAMAP; MF_01190; HTH_type_FabR; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR023764; Tscrpt_reg_HTH_FabR.
DR Pfam; PF00440; TetR_N; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..234
FT /note="HTH-type transcriptional repressor FabR"
FT /id="PRO_0000070641"
FT DOMAIN 29..89
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 52..71
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT VARIANT 61
FT /note="G -> V (in strain: K12 / BW25113, may not bind DNA)"
FT /evidence="ECO:0000305|PubMed:19854834"
FT CONFLICT 47
FT /note="S -> T (in Ref. 1; CAA46823)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="G -> V (in Ref. 1; CAA46823)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..89
FT /note="ML -> IV (in Ref. 1; CAA46823)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..94
FT /note="MR -> IG (in Ref. 1; CAA46823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26553 MW; 326336C26008274E CRC64;
MFILWYSASS TFGKDSDIVM GVRAQQKEKT RRSLVEAAFS QLSAERSFAS LSLREVAREA
GIAPTSFYRH FRDVDELGLT MVDESGLMLR QLMRQARQRI AKGGSVIRTS VSTFMEFIGN
NPNAFRLLLR ERSGTSAAFR AAVAREIQHF IAELADYLEL ENHMPRAFTE AQAEAMVTIV
FSAGAEALDV GVEQRRQLEE RLVLQLRMIS KGAYYWYRRE QEKTAIIPGN VKDE
