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 05-MAY-2009, entry version 59.
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.
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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; -.
DR PDB; 1VI0; X-ray; 1.65 A; A/B=1-194.
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; P94548; CGRAPRK.
DR BioCyc; BSUB224308:BSU2851-MON; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 InterPro; IPR012287; Homeodomain-rel.
DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_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).
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
//