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 11-JUN-2014, entry version 101. 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; 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 RT subtilis chromosome containing genes responsible for stress responses, RT the 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., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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., RA Watanabe K., 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., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA 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 CC and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, CC fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is CC specifically inhibited by long chain fatty acyl-CoA compounds of CC 14-20 carbon atoms in length. CC -!- SUBUNIT: Homodimer. Binds to DNA. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. 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; 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 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 ProteinModelPortal; P94548; -. DR SMR; P94548; 6-194. DR STRING; 224308.BSU28550; -. DR PaxDb; P94548; -. DR EnsemblBacteria; CAB14815; CAB14815; BSU28550. DR GeneID; 938105; -. DR KEGG; bsu:BSU28550; -. DR PATRIC; 18977598; VBIBacSub10457_2987. DR GenoList; BSU28550; -. DR eggNOG; COG1309; -. DR HOGENOM; HOG000012954; -. DR KO; K13770; -. DR OMA; TWVMNDQ; -. DR OrthoDB; EOG6PP9N1; -. DR BioCyc; BSUB:BSU28550-MONOMER; -. DR EvolutionaryTrace; P94548; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 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; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR Gene3D; 1.10.357.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR InterPro; IPR011075; Tet_transcr_reg_TetR-rel_C. 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; Complete proteome; Cytoplasm; DNA-binding; KW Fatty acid metabolism; Lipid degradation; Lipid metabolism; KW Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 194 Fatty acid metabolism regulator protein. FT /FTId=PRO_0000360674. FT DOMAIN 5 65 HTH tetR-type. FT DNA_BIND 28 47 H-T-H motif (By similarity). FT HELIX 7 22 FT HELIX 24 26 FT HELIX 29 36 FT HELIX 40 46 FT HELIX 50 73 FT HELIX 79 95 FT HELIX 98 105 FT TURN 106 108 FT HELIX 113 139 FT STRAND 141 143 FT HELIX 149 169 FT TURN 170 172 FT HELIX 176 179 FT HELIX 180 189 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 //