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Protein

Arabinose metabolism transcriptional repressor

Gene

araR

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

Functioni

Transcriptional repressor of the arabinose utilization genes. Also regulates its own expression. Binds to two sequences within the promoters of the araABDLMNPQ-abfA operon and the araE gene, and to one sequence in the araR promoter.

Enzyme regulationi

Binding to DNA is inhibited by L-arabinose.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi30 – 4920H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU33970-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Arabinose metabolism transcriptional repressor
Gene namesi
Name:araR
Synonyms:araC, yvbS
Ordered Locus Names:BSU33970
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU33970. [Micado]

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Arabinose metabolism transcriptional repressorPRO_0000050620Add
BLAST

Proteomic databases

PaxDbiP96711.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU33970.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1714Combined sources
Helixi30 – 378Combined sources
Helixi41 – 5313Combined sources
Beta strandi56 – 605Combined sources
Turni61 – 633Combined sources
Beta strandi64 – 674Combined sources
Beta strandi81 – 877Combined sources
Beta strandi89 – 913Combined sources
Helixi94 – 10714Combined sources
Beta strandi111 – 1166Combined sources
Helixi121 – 13313Combined sources
Beta strandi137 – 1415Combined sources
Helixi153 – 1619Combined sources
Beta strandi166 – 1716Combined sources
Beta strandi180 – 1834Combined sources
Helixi185 – 19814Combined sources
Beta strandi203 – 21210Combined sources
Helixi213 – 22816Combined sources
Helixi235 – 2373Combined sources
Beta strandi238 – 2414Combined sources
Helixi243 – 2464Combined sources
Helixi249 – 26012Combined sources
Turni261 – 2633Combined sources
Beta strandi267 – 2704Combined sources
Helixi274 – 28613Combined sources
Turni291 – 2944Combined sources
Beta strandi296 – 2983Combined sources
Helixi305 – 3084Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi314 – 3174Combined sources
Helixi321 – 33515Combined sources
Beta strandi345 – 3473Combined sources
Beta strandi350 – 3523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TB6X-ray2.21A/B71-362[»]
4EGYX-ray2.30A/B1-68[»]
4EGZX-ray2.30A/B1-68[»]
4H0EX-ray1.97A/B1-68[»]
ProteinModelPortaliP96711.
SMRiP96711. Positions 2-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7070HTH gntR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1609.
HOGENOMiHOG000235268.
InParanoidiP96711.
OMAiAIMELEF.
OrthoDBiEOG64BQ72.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR028082. Peripla_BP_I.
IPR000524. Tscrpt_reg_HTH_GntR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00392. GntR. 1 hit.
[Graphical view]
PRINTSiPR00035. HTHGNTR.
SMARTiSM00345. HTH_GNTR. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
PROSITEiPS50949. HTH_GNTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P96711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPKYAQVKE EISSWINQGK ILPDQKIPTE NELMQQFGVS RHTIRKAIGD
60 70 80 90 100
LVSQGLLYSV QGGGTFVASR SAKSALHSNK TIGVLTTYIS DYIFPSIIRG
110 120 130 140 150
IESYLSEQGY SMLLTSTNNN PDNERRGLEN LLSQHIDGLI VEPTKSALQT
160 170 180 190 200
PNIGYYLNLE KNGIPFAMIN ASYAELAAPS FTLDDVKGGM MAAEHLLSLG
210 220 230 240 250
HTHMMGIFKA DDTQGVKRMN GFIQAHRERE LFPSPDMIVT FTTEEKESKL
260 270 280 290 300
LEKVKATLEK NSKHMPTAIL CYNDEIALKV IDMLREMDLK VPEDMSIVGY
310 320 330 340 350
DDSHFAQISE VKLTSVKHPK SVLGKAAAKY VIDCLEHKKP KQEDVIFEPE
360
LIIRQSARKL NE
Length:362
Mass (Da):40,488
Last modified:April 2, 2002 - v3
Checksum:i679DC8FEE69FB421
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98354 Genomic DNA. Translation: CAA66999.1.
AL009126 Genomic DNA. Translation: CAB15402.2.
PIRiD69588.

Genome annotation databases

EnsemblBacteriaiCAB15402; CAB15402; BSU33970.
PATRICi18978794. VBIBacSub10457_3560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98354 Genomic DNA. Translation: CAA66999.1.
AL009126 Genomic DNA. Translation: CAB15402.2.
PIRiD69588.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TB6X-ray2.21A/B71-362[»]
4EGYX-ray2.30A/B1-68[»]
4EGZX-ray2.30A/B1-68[»]
4H0EX-ray1.97A/B1-68[»]
ProteinModelPortaliP96711.
SMRiP96711. Positions 2-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU33970.

Proteomic databases

PaxDbiP96711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15402; CAB15402; BSU33970.
PATRICi18978794. VBIBacSub10457_3560.

Organism-specific databases

GenoListiBSU33970. [Micado]

Phylogenomic databases

eggNOGiCOG1609.
HOGENOMiHOG000235268.
InParanoidiP96711.
OMAiAIMELEF.
OrthoDBiEOG64BQ72.

Enzyme and pathway databases

BioCyciBSUB:BSU33970-MONOMER.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR028082. Peripla_BP_I.
IPR000524. Tscrpt_reg_HTH_GntR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00392. GntR. 1 hit.
[Graphical view]
PRINTSiPR00035. HTHGNTR.
SMARTiSM00345. HTH_GNTR. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
PROSITEiPS50949. HTH_GNTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Negative regulation of L-arabinose metabolism in Bacillus subtilis: characterization of the araR (araC) gene."
    Sa-Nogueira I.M.G., Mota L.J.
    J. Bacteriol. 179:1598-1608(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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis."
    Mota L.J., Tavares P., Sa-Nogueira I.M.G.
    Mol. Microbiol. 33:476-489(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION.
  4. "Control of the arabinose regulon in Bacillus subtilis by AraR in vivo: crucial roles of operators, cooperativity, and DNA looping."
    Mota L.J., Sarmento L.M., Sa-Nogueira I.M.G.
    J. Bacteriol. 183:4190-4201(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: 168.

Entry informationi

Entry nameiARAR_BACSU
AccessioniPrimary (citable) accession number: P96711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 2, 2002
Last sequence update: April 2, 2002
Last modified: January 6, 2015
This is version 100 of the entry and version 3 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

External Data

Dasty 3

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 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.