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Protein

Transcription factor FapR

Gene

fapR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor involved in regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism. Binds to the 5'-TTAGTANNNNNTANTAA-3' consensus sequence found in the promoter of fabHAF operon (containing fabHA and fabF genes), yhdO and fapR genes and prevents their expression. Its action is probably modulated by malonyl-CoA.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU15880-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor FapR
Alternative name(s):
Fatty acid and phospholipid biosynthesis regulator
Gene namesi
Name:fapR
Synonyms:ylpC
Ordered Locus Names:BSU15880
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Transcription factor FapRPRO_0000172819Add
BLAST

Proteomic databases

PaxDbiO34835.

Expressioni

Inductioni

Autoregulated.1 Publication

Interactioni

Protein-protein interaction databases

IntActiO34835. 6 interactions.
STRINGi224308.Bsubs1_010100008761.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 6317Combined sources
Helixi71 – 733Combined sources
Beta strandi75 – 828Combined sources
Turni83 – 853Combined sources
Beta strandi86 – 927Combined sources
Helixi95 – 973Combined sources
Turni100 – 1023Combined sources
Helixi107 – 12014Combined sources
Beta strandi129 – 1368Combined sources
Beta strandi145 – 15511Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi162 – 1709Combined sources
Beta strandi173 – 18210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F3XX-ray3.10A/B44-188[»]
2F41X-ray2.50A/B/C/D68-188[»]
ProteinModelPortaliO34835.
SMRiO34835. Positions 44-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34835.

Family & Domainsi

Sequence similaritiesi

Belongs to the FapR family.Curated

Phylogenomic databases

eggNOGiENOG4108VVV. Bacteria.
COG2050. LUCA.
HOGENOMiHOG000095867.
OMAiCIAKAYV.
OrthoDBiEOG6RNQD8.
PhylomeDBiO34835.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_01814. Transcrip_fact_FapR.
InterProiIPR029069. HotDog_dom.
IPR017275. Transcription_factor_FapR.
[Graphical view]
PIRSFiPIRSF037733. Transcription_factor_FapR. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.

Sequencei

Sequence statusi: Complete.

O34835-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRNKRERQE LLQQTIQATP FITDEELAGK FGVSIQTIRL DRLELSIPEL
60 70 80 90 100
RERIKNVAEK TLEDEVKSLS LDEVIGEIID LELDDQAISI LEIKQEHVFS
110 120 130 140 150
RNQIARGHHL FAQANSLAVA VIDDELALTA SADIRFTRQV KQGERVVAKA
160 170 180
KVTAVEKEKG RTVVEVNSYV GEEIVFSGRF DMYRSKHS
Length:188
Mass (Da):21,400
Last modified:January 1, 1998 - v1
Checksum:iCF38F3781C20BD63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13937 Genomic DNA. Translation: CAA74247.1.
AL009126 Genomic DNA. Translation: CAB13461.1.
PIRiA69880.
RefSeqiNP_389470.1. NC_000964.3.
WP_003232044.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13461; CAB13461; BSU15880.
GeneIDi936595.
KEGGibsu:BSU15880.
PATRICi18974981. VBIBacSub10457_1682.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13937 Genomic DNA. Translation: CAA74247.1.
AL009126 Genomic DNA. Translation: CAB13461.1.
PIRiA69880.
RefSeqiNP_389470.1. NC_000964.3.
WP_003232044.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F3XX-ray3.10A/B44-188[»]
2F41X-ray2.50A/B/C/D68-188[»]
ProteinModelPortaliO34835.
SMRiO34835. Positions 44-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO34835. 6 interactions.
STRINGi224308.Bsubs1_010100008761.

Proteomic databases

PaxDbiO34835.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13461; CAB13461; BSU15880.
GeneIDi936595.
KEGGibsu:BSU15880.
PATRICi18974981. VBIBacSub10457_1682.

Phylogenomic databases

eggNOGiENOG4108VVV. Bacteria.
COG2050. LUCA.
HOGENOMiHOG000095867.
OMAiCIAKAYV.
OrthoDBiEOG6RNQD8.
PhylomeDBiO34835.

Enzyme and pathway databases

BioCyciBSUB:BSU15880-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO34835.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_01814. Transcrip_fact_FapR.
InterProiIPR029069. HotDog_dom.
IPR017275. Transcription_factor_FapR.
[Graphical view]
PIRSFiPIRSF037733. Transcription_factor_FapR. 1 hit.
SUPFAMiSSF54637. SSF54637. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome."
    Foulger D., Errington J.
    Microbiology 144:801-805(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis."
    Schujman G.E., Paoletti L., Grossman A.D., de Mendoza D.
    Dev. Cell 4:663-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-9, FUNCTION, DNA-BINDING, INDUCTION.

Entry informationi

Entry nameiFAPR_BACSU
AccessioniPrimary (citable) accession number: O34835
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.