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Protein

Fatty acid metabolism regulator protein

Gene

fadR

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

Functioni

Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi28 – 4720H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU28550-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid metabolism regulator protein
Gene namesi
Name:fadR
Synonyms:ysiA
Ordered Locus Names:BSU28550
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Fatty acid metabolism regulator proteinPRO_0000360674Add
BLAST

Proteomic databases

PaxDbiP94548.

Interactioni

Subunit structurei

Homodimer. Binds to DNA.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015586.

Structurei

Secondary structure

1
194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2216Combined sources
Helixi24 – 263Combined sources
Helixi29 – 368Combined sources
Helixi40 – 467Combined sources
Helixi50 – 7324Combined sources
Helixi79 – 9517Combined sources
Helixi98 – 1058Combined sources
Turni106 – 1083Combined sources
Helixi113 – 13927Combined sources
Beta strandi141 – 1433Combined sources
Helixi149 – 16921Combined sources
Turni170 – 1723Combined sources
Helixi176 – 1794Combined sources
Helixi180 – 18910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VI0X-ray1.65A/B2-194[»]
3WHBX-ray2.15A/B1-194[»]
3WHCX-ray2.20A/B/C/D/E/F1-194[»]
ProteinModelPortaliP94548.
SMRiP94548. Positions 6-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP94548.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6561HTH tetR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH tetR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107Z3H. Bacteria.
ENOG411032B. LUCA.
HOGENOMiHOG000012954.
InParanoidiP94548.
KOiK13770.
OMAiKGYLNML.
OrthoDBiEOG6PP9N1.
PhylomeDBiP94548.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.357.10. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
IPR013570. Tscrpt_reg_YsiA_C.
[Graphical view]
PfamiPF08359. TetR_C_4. 1 hit.
PF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF48498. SSF48498. 1 hit.
PROSITEiPS50977. HTH_TETR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P94548-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQKRPKYMQ IIDAAVEVIA ENGYHQSQVS KIAKQAGVAD GTIYLYFKNK
60 70 80 90 100
EDILISLFKE KMGQFIERME EDIKEKATAK EKLALVISKH FSLLAGDHNL
110 120 130 140 150
AIVTQLELRQ SNLELRQKIN EILKGYLNIL DGILTEGIQS GEIKEGLDVR
160 170 180 190
LARQMIFGTI DETVTTWVMN DQKYDLVALS NSVLELLVSG IHNK
Length:194
Mass (Da):21,979
Last modified:May 1, 1997 - v1
Checksum:iA8C01C9C3B47CFE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99572.1.
AL009126 Genomic DNA. Translation: CAB14815.1.
PIRiF69985.
RefSeqiNP_390733.1. NC_000964.3.
WP_003229547.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14815; CAB14815; BSU28550.
GeneIDi938105.
KEGGibsu:BSU28550.
PATRICi18977598. VBIBacSub10457_2987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99572.1.
AL009126 Genomic DNA. Translation: CAB14815.1.
PIRiF69985.
RefSeqiNP_390733.1. NC_000964.3.
WP_003229547.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VI0X-ray1.65A/B2-194[»]
3WHBX-ray2.15A/B1-194[»]
3WHCX-ray2.20A/B/C/D/E/F1-194[»]
ProteinModelPortaliP94548.
SMRiP94548. Positions 6-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015586.

Proteomic databases

PaxDbiP94548.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14815; CAB14815; BSU28550.
GeneIDi938105.
KEGGibsu:BSU28550.
PATRICi18977598. VBIBacSub10457_2987.

Phylogenomic databases

eggNOGiENOG4107Z3H. Bacteria.
ENOG411032B. LUCA.
HOGENOMiHOG000012954.
InParanoidiP94548.
KOiK13770.
OMAiKGYLNML.
OrthoDBiEOG6PP9N1.
PhylomeDBiP94548.

Enzyme and pathway databases

BioCyciBSUB:BSU28550-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP94548.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.357.10. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
IPR013570. Tscrpt_reg_YsiA_C.
[Graphical view]
PfamiPF08359. TetR_C_4. 1 hit.
PF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF48498. SSF48498. 1 hit.
PROSITEiPS50977. HTH_TETR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism."
    Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.
    Microbiology 142:3067-3078(1996) [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. "Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation."
    Matsuoka H., Hirooka K., Fujita Y.
    J. Biol. Chem. 282:5180-5194(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DNA-BINDING, GENE NAME.
    Strain: 168.
  4. Cited for: REVIEW, GENE FAMILY.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Entry informationi

Entry nameiFADR_BACSU
AccessioniPrimary (citable) accession number: P94548
Secondary accession number(s): Q795X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 1, 1997
Last modified: February 17, 2016
This is version 115 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, 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.