ID   FABR_YERPS              Reviewed;         211 AA.
AC   Q66G60;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=HTH-type transcriptional repressor FabR {ECO:0000255|HAMAP-Rule:MF_01190};
GN   Name=fabR {ECO:0000255|HAMAP-Rule:MF_01190}; OrderedLocusNames=YPTB0122;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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=CAH19362.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX936398; CAH19362.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002209476.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66G60; -.
DR   SMR; Q66G60; -.
DR   EnsemblBacteria; CAH19362; CAH19362; YPTB0122.
DR   GeneID; 66843485; -.
DR   KEGG; ypo:BZ17_2474; -.
DR   KEGG; yps:YPTB0122; -.
DR   PATRIC; fig|273123.14.peg.2593; -.
DR   OMA; REHWRFI; -.
DR   Proteomes; UP000001011; 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..211
FT                   /note="HTH-type transcriptional repressor FabR"
FT                   /id="PRO_0000293582"
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   211 AA;  24167 MW;  E70A14DEE10B9304 CRC64;
     MGVRAQQKER TRRSLIEAAF SQLSAERSFA SLSLREVSRE AGIAPTSFYR HFRDVDELGL
     TMVDESGLML RQLMRQARQR IAKGGSVIRT SVSTFMEFIG NNPNAFRLLL RERSGTSAAF
     RAAVAREIQH FIAELADYLE LENHMPRSFT EAQAEAMVTI VFSAGAEVLD VDIEQRRQLE
     ERLVLQLRMI SKGAYYWYRR EQEKLAASRV E