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 24-NOV-2009, entry version 65. DE RecName: Full=Fatty acid metabolism regulator protein; GN Name=fadR; Synonyms=ysiA; OrderedLocusNames=BSU28550; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=97124191; 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 MEDLINE=98044033; 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; -. DR PDB; 1VI0; X-ray; 1.65 A; A/B=2-194. DR PDBsum; 1VI0; -. DR GeneID; 938105; -. DR GenomeReviews; AL009126_GR; BSU28550. DR KEGG; bsu:BSU28550; -. DR NMPDR; fig|224308.1.peg.2858; -. DR SubtiList; BG12330; fadR. DR HOGENOM; P94548; -. DR OMA; VKGESAT; -. DR BioCyc; SUBTI:BSU28550-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016566; F:specific transcriptional repressor activity; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity; IEA:InterPro. 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:0016481; P:negative regulation of transcription; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR InterPro; IPR011075; Tet_transcr_reg_TetR-rel_C. DR InterPro; IPR001647; Transcr-reg_TetR-like_bac/arc. DR InterPro; IPR013570; Transcr_reg_YsiA_C. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Gene3D; G3DSA:1.10.357.10; TetR_C; 1. DR Pfam; PF08359; TetR_C_4; 1. DR Pfam; PF00440; TetR_N; 1. DR PRINTS; PR00455; HTHTETR. DR PROSITE; PS01081; HTH_TETR_1; FALSE_NEG. 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; Repressor; KW Transcription; 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 21 FT HELIX 29 35 FT HELIX 43 46 FT HELIX 50 61 FT HELIX 65 73 FT HELIX 79 94 FT HELIX 98 105 FT TURN 106 108 FT HELIX 113 123 FT HELIX 127 130 FT HELIX 149 156 FT HELIX 160 169 FT TURN 170 172 FT HELIX 176 179 FT HELIX 180 188 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 //