ID   FABR_ECOL6              Reviewed;         215 AA.
AC   Q8FB90;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=HTH-type transcriptional repressor FabR {ECO:0000255|HAMAP-Rule:MF_01190};
GN   Name=fabR {ECO:0000255|HAMAP-Rule:MF_01190}; OrderedLocusNames=c4926;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Represses the transcription of fabB, involved in unsaturated
CC       fatty acid (UFA) biosynthesis. By controlling UFA production, FabR
CC       directly influences the physical properties of the membrane bilayer.
CC       {ECO:0000255|HAMAP-Rule:MF_01190}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01190}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE014075; AAN83354.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8FB90; -.
DR   SMR; Q8FB90; -.
DR   STRING; 199310.c4926; -.
DR   EnsemblBacteria; AAN83354; AAN83354; c4926.
DR   KEGG; ecc:c4926; -.
DR   eggNOG; COG1309; Bacteria.
DR   HOGENOM; CLU_081861_0_0_6; -.
DR   Proteomes; UP000001410; 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; IEA:UniProtKB-UniRule.
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   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   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..215
FT                   /note="HTH-type transcriptional repressor FabR"
FT                   /id="PRO_0000293568"
FT   DOMAIN          10..70
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01190"
FT   DNA_BIND        33..52
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01190"
SQ   SEQUENCE   215 AA;  24434 MW;  ACB9729EA947E256 CRC64;
     MGVRAQQKEK TRRSLVEAAF SQLSAERSFA SLSLREVARE AGIAPTSFYR HFRDVDELGL
     TMVDESGLML RQLMRQARQR IAKGGSVIRT SVSTFMEFIG NNPNAFRLLL RERSGTSAAF
     RAAVAREIQH FIAELADYLE LENHMPRAFT EAQAEAMVTI VFSAGAEALD VGVEQRRQLE
     ERLVLQLRMI SKGAYYWYRR EQEKTTIIPG NVKDE