FADR_BACSU
ID FADR_BACSU Reviewed; 194 AA.
AC P94548; Q795X6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Fatty acid metabolism regulator protein;
GN Name=fadR; Synonyms=ysiA; OrderedLocusNames=BSU28550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, SUBUNIT, DNA-BINDING, AND GENE NAME.
RC STRAIN=168;
RX PubMed=17189250; DOI=10.1074/jbc.m606831200;
RA Matsuoka H., Hirooka K., Fujita Y.;
RT "Organization and function of the YsiA regulon of Bacillus subtilis
RT involved in fatty acid degradation.";
RL J. Biol. Chem. 282:5180-5194(2007).
RN [4]
RP REVIEW, AND GENE FAMILY.
RX PubMed=15944459; DOI=10.1128/mmbr.69.2.326-356.2005;
RA Ramos J.L., Martinez-Bueno M., Molina-Henares A.J., Teran W., Watanabe K.,
RA Zhang X., Gallegos M.T., Brennan R., Tobes R.;
RT "The TetR family of transcriptional repressors.";
RL Microbiol. Mol. Biol. Rev. 69:326-356(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Transcriptional regulator in fatty acid degradation.
CC Represses transcription of genes required for fatty acid transport and
CC beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH,
CC fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically
CC inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms
CC in length. {ECO:0000269|PubMed:17189250}.
CC -!- SUBUNIT: Homodimer. Binds to DNA. {ECO:0000269|PubMed:17189250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; Z75208; CAA99572.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14815.1; -; Genomic_DNA.
DR PIR; F69985; F69985.
DR RefSeq; NP_390733.1; NC_000964.3.
DR RefSeq; WP_003229547.1; NZ_JNCM01000036.1.
DR PDB; 1VI0; X-ray; 1.65 A; A/B=2-194.
DR PDB; 3WHB; X-ray; 2.15 A; A/B=1-194.
DR PDB; 3WHC; X-ray; 2.20 A; A/B/C/D/E/F=1-194.
DR PDBsum; 1VI0; -.
DR PDBsum; 3WHB; -.
DR PDBsum; 3WHC; -.
DR AlphaFoldDB; P94548; -.
DR SMR; P94548; -.
DR STRING; 224308.BSU28550; -.
DR DrugBank; DB03264; Dodecyl-Coa.
DR jPOST; P94548; -.
DR PaxDb; P94548; -.
DR PRIDE; P94548; -.
DR EnsemblBacteria; CAB14815; CAB14815; BSU_28550.
DR GeneID; 938105; -.
DR KEGG; bsu:BSU28550; -.
DR PATRIC; fig|224308.179.peg.3102; -.
DR eggNOG; COG1309; Bacteria.
DR InParanoid; P94548; -.
DR OMA; CRIADVA; -.
DR PhylomeDB; P94548; -.
DR BioCyc; BSUB:BSU28550-MON; -.
DR EvolutionaryTrace; P94548; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR InterPro; IPR013570; Tscrpt_reg_YsiA_C.
DR Pfam; PF08359; TetR_C_4; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48498; SSF48498; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Fatty acid metabolism;
KW Lipid degradation; Lipid metabolism; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..194
FT /note="Fatty acid metabolism regulator protein"
FT /id="PRO_0000360674"
FT DOMAIN 5..65
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 28..47
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 50..73
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:1VI0"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 113..139
FT /evidence="ECO:0007829|PDB:1VI0"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3WHC"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:1VI0"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1VI0"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:1VI0"
SQ SEQUENCE 194 AA; 21979 MW; A8C01C9C3B47CFE8 CRC64;
MKQKRPKYMQ IIDAAVEVIA ENGYHQSQVS KIAKQAGVAD GTIYLYFKNK EDILISLFKE
KMGQFIERME EDIKEKATAK EKLALVISKH FSLLAGDHNL AIVTQLELRQ SNLELRQKIN
EILKGYLNIL DGILTEGIQS GEIKEGLDVR LARQMIFGTI DETVTTWVMN DQKYDLVALS
NSVLELLVSG IHNK
