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Database: UniProt
Entry: O34835
LinkDB: O34835
Original site: O34835 
ID   FAPR_BACSU              Reviewed;         188 AA.
AC   O34835;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-JUN-2021, entry version 124.
DE   RecName: Full=Transcription factor FapR;
DE   AltName: Full=Fatty acid and phospholipid biosynthesis regulator;
GN   Name=fapR; Synonyms=ylpC; OrderedLocusNames=BSU15880;
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=9534248; DOI=10.1099/00221287-144-3-801;
RA   Foulger D., Errington J.;
RT   "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT   genome.";
RL   Microbiology 144:801-805(1998).
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   PROTEIN SEQUENCE OF 1-9, FUNCTION, DNA-BINDING, AND INDUCTION.
RX   PubMed=12737802; DOI=10.1016/s1534-5807(03)00123-0;
RA   Schujman G.E., Paoletti L., Grossman A.D., de Mendoza D.;
RT   "FapR, a bacterial transcription factor involved in global regulation of
RT   membrane lipid biosynthesis.";
RL   Dev. Cell 4:663-672(2003).
CC   -!- FUNCTION: Transcription factor involved in regulation of membrane lipid
CC       biosynthesis by repressing genes involved in fatty acid and
CC       phospholipid metabolism. Binds to the 5'-TTAGTANNNNNTANTAA-3' consensus
CC       sequence found in the promoter of fabHAF operon (containing fabHA and
CC       fabF genes), yhdO and fapR genes and prevents their expression. Its
CC       action is probably modulated by malonyl-CoA.
CC       {ECO:0000269|PubMed:12737802}.
CC   -!- INDUCTION: Autoregulated. {ECO:0000269|PubMed:12737802}.
CC   -!- SIMILARITY: Belongs to the FapR family. {ECO:0000305}.
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DR   EMBL; Y13937; CAA74247.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13461.1; -; Genomic_DNA.
DR   PIR; A69880; A69880.
DR   RefSeq; NP_389470.1; NC_000964.3.
DR   RefSeq; WP_003232044.1; NZ_JNCM01000035.1.
DR   PDB; 2F3X; X-ray; 3.10 A; A/B=44-188.
DR   PDB; 2F41; X-ray; 2.50 A; A/B/C/D=68-188.
DR   PDBsum; 2F3X; -.
DR   PDBsum; 2F41; -.
DR   SMR; O34835; -.
DR   IntAct; O34835; 6.
DR   STRING; 224308.BSU15880; -.
DR   PaxDb; O34835; -.
DR   EnsemblBacteria; CAB13461; CAB13461; BSU_15880.
DR   GeneID; 936595; -.
DR   KEGG; bsu:BSU15880; -.
DR   PATRIC; fig|224308.179.peg.1728; -.
DR   eggNOG; COG1349; Bacteria.
DR   eggNOG; COG2050; Bacteria.
DR   OMA; GIARGHH; -.
DR   PhylomeDB; O34835; -.
DR   BioCyc; BSUB:BSU15880-MONOMER; -.
DR   EvolutionaryTrace; O34835; -.
DR   Proteomes; UP000001570; Chromosome.
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-KW.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_01814; Transcrip_fact_FapR; 1.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR006683; Thioestr_dom.
DR   InterPro; IPR017275; Transcription_factor_FapR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF03061; 4HBT; 1.
DR   PIRSF; PIRSF037733; Transcription_factor_FapR; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA-binding;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..188
FT                   /note="Transcription factor FapR"
FT                   /id="PRO_0000172819"
FT   HELIX           47..63
FT                   /evidence="ECO:0007829|PDB:2F3X"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:2F3X"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:2F3X"
FT   HELIX           107..120
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   STRAND          129..136
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   STRAND          145..155
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   STRAND          162..170
FT                   /evidence="ECO:0007829|PDB:2F41"
FT   STRAND          173..182
FT                   /evidence="ECO:0007829|PDB:2F41"
SQ   SEQUENCE   188 AA;  21400 MW;  CF38F3781C20BD63 CRC64;
     MRRNKRERQE LLQQTIQATP FITDEELAGK FGVSIQTIRL DRLELSIPEL RERIKNVAEK
     TLEDEVKSLS LDEVIGEIID LELDDQAISI LEIKQEHVFS RNQIARGHHL FAQANSLAVA
     VIDDELALTA SADIRFTRQV KQGERVVAKA KVTAVEKEKG RTVVEVNSYV GEEIVFSGRF
     DMYRSKHS
//
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