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Protein

Arabinose operon regulatory protein

Gene

araC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This protein controls the expression of at least six genes that are involved in the transport and catabolism of L-arabinose. It regulates initiation of transcription of the araBAD operon and it also controls its own synthesis. The L-arabinose operon displays both positive and negative regulation through AraC.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi197 – 21620H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • arabinose catabolic process Source: EcoliWiki
  • regulation of transcription, DNA-templated Source: GO_Central
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Arabinose catabolism, Carbohydrate metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00242.
ECOL316407:JW0063-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Arabinose operon regulatory protein
Gene namesi
Name:araC
Ordered Locus Names:b0064, JW0063
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10054. araC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Arabinose operon regulatory proteinPRO_0000194499Add
BLAST

Proteomic databases

PaxDbiP0A9E0.

Expressioni

Gene expression databases

CollecTFiEXPREG_000007d0.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
xerCP0A8P63EBI-1113479,EBI-1133806

Protein-protein interaction databases

BioGridi4260828. 116 interactions.
DIPiDIP-9125N.
IntActiP0A9E0. 12 interactions.
STRINGi511145.b0064.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 133Combined sources
Beta strandi16 – 183Combined sources
Beta strandi20 – 278Combined sources
Beta strandi36 – 383Combined sources
Beta strandi43 – 5311Combined sources
Beta strandi55 – 595Combined sources
Beta strandi62 – 665Combined sources
Beta strandi71 – 744Combined sources
Beta strandi80 – 845Combined sources
Beta strandi88 – 9811Combined sources
Helixi102 – 1076Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi117 – 1204Combined sources
Turni124 – 1263Combined sources
Helixi127 – 14216Combined sources
Beta strandi145 – 1473Combined sources
Helixi148 – 16619Combined sources
Helixi177 – 18812Combined sources
Helixi197 – 2037Combined sources
Helixi208 – 21912Combined sources
Helixi223 – 24119Combined sources
Helixi246 – 2527Combined sources
Helixi258 – 26912Combined sources
Helixi273 – 2786Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XJAX-ray2.40A/B/C/D/E1-178[»]
2AACX-ray1.60A/B2-178[»]
2ARAX-ray2.80A19-167[»]
2ARCX-ray1.50A/B7-170[»]
2K9SNMR-A175-281[»]
ProteinModelPortaliP0A9E0.
SMRiP0A9E0. Positions 7-170, 175-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9E0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – ?Dimerization

Sequence similaritiesi

Contains 1 HTH araC/xylS-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG41063TF. Bacteria.
ENOG4111G16. LUCA.
HOGENOMiHOG000276603.
InParanoidiP0A9E0.
KOiK02099.
OMAiGFEDQLY.
OrthoDBiEOG6K3ZZH.
PhylomeDBiP0A9E0.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
2.60.120.280. 1 hit.
InterProiIPR003313. AraC-bd.
IPR009057. Homeodomain-like.
IPR018060. HTH_AraC.
IPR018062. HTH_AraC-typ_CS.
IPR020449. Tscrpt_reg_HTH_AraC-type.
[Graphical view]
PfamiPF02311. AraC_binding. 1 hit.
PF12833. HTH_18. 1 hit.
[Graphical view]
PRINTSiPR00032. HTHARAC.
SMARTiSM00342. HTH_ARAC. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
SSF51215. SSF51215. 1 hit.
PROSITEiPS00041. HTH_ARAC_FAMILY_1. 1 hit.
PS01124. HTH_ARAC_FAMILY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9E0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAQNDPLL PGYSFNAHLV AGLTPIEANG YLDFFIDRPL GMKGYILNLT
60 70 80 90 100
IRGQGVVKNQ GREFVCRPGD ILLFPPGEIH HYGRHPEARE WYHQWVYFRP
110 120 130 140 150
RAYWHEWLNW PSIFANTGFF RPDEAHQPHF SDLFGQIINA GQGEGRYSEL
160 170 180 190 200
LAINLLEQLL LRRMEAINES LHPPMDNRVR EACQYISDHL ADSNFDIASV
210 220 230 240 250
AQHVCLSPSR LSHLFRQQLG ISVLSWREDQ RISQAKLLLS TTRMPIATVG
260 270 280 290
RNVGFDDQLY FSRVFKKCTG ASPSEFRAGC EEKVNDVAVK LS
Length:292
Mass (Da):33,384
Last modified:July 21, 1986 - v1
Checksum:iC5A737E285A4ECC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71D → E in AAA23468 (PubMed:6160371).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00256 Genomic DNA. Translation: CAA23507.1.
V00259 Genomic DNA. Translation: CAA23508.1.
J01641 Genomic DNA. Translation: AAA23466.1.
U00096 Genomic DNA. Translation: AAC73175.1.
AP009048 Genomic DNA. Translation: BAB96633.1.
K01303 Genomic DNA. Translation: AAA23468.1.
PIRiA91473. RGECA.
RefSeqiNP_414606.1. NC_000913.3.
WP_001300811.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73175; AAC73175; b0064.
BAB96633; BAB96633; BAB96633.
GeneIDi944780.
KEGGiecj:JW0063.
eco:b0064.
PATRICi32115229. VBIEscCol129921_0066.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00256 Genomic DNA. Translation: CAA23507.1.
V00259 Genomic DNA. Translation: CAA23508.1.
J01641 Genomic DNA. Translation: AAA23466.1.
U00096 Genomic DNA. Translation: AAC73175.1.
AP009048 Genomic DNA. Translation: BAB96633.1.
K01303 Genomic DNA. Translation: AAA23468.1.
PIRiA91473. RGECA.
RefSeqiNP_414606.1. NC_000913.3.
WP_001300811.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XJAX-ray2.40A/B/C/D/E1-178[»]
2AACX-ray1.60A/B2-178[»]
2ARAX-ray2.80A19-167[»]
2ARCX-ray1.50A/B7-170[»]
2K9SNMR-A175-281[»]
ProteinModelPortaliP0A9E0.
SMRiP0A9E0. Positions 7-170, 175-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260828. 116 interactions.
DIPiDIP-9125N.
IntActiP0A9E0. 12 interactions.
STRINGi511145.b0064.

Proteomic databases

PaxDbiP0A9E0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73175; AAC73175; b0064.
BAB96633; BAB96633; BAB96633.
GeneIDi944780.
KEGGiecj:JW0063.
eco:b0064.
PATRICi32115229. VBIEscCol129921_0066.

Organism-specific databases

EchoBASEiEB0052.
EcoGeneiEG10054. araC.

Phylogenomic databases

eggNOGiENOG41063TF. Bacteria.
ENOG4111G16. LUCA.
HOGENOMiHOG000276603.
InParanoidiP0A9E0.
KOiK02099.
OMAiGFEDQLY.
OrthoDBiEOG6K3ZZH.
PhylomeDBiP0A9E0.

Enzyme and pathway databases

BioCyciEcoCyc:PD00242.
ECOL316407:JW0063-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A9E0.
PROiP0A9E0.

Gene expression databases

CollecTFiEXPREG_000007d0.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
2.60.120.280. 1 hit.
InterProiIPR003313. AraC-bd.
IPR009057. Homeodomain-like.
IPR018060. HTH_AraC.
IPR018062. HTH_AraC-typ_CS.
IPR020449. Tscrpt_reg_HTH_AraC-type.
[Graphical view]
PfamiPF02311. AraC_binding. 1 hit.
PF12833. HTH_18. 1 hit.
[Graphical view]
PRINTSiPR00032. HTHARAC.
SMARTiSM00342. HTH_ARAC. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
SSF51215. SSF51215. 1 hit.
PROSITEiPS00041. HTH_ARAC_FAMILY_1. 1 hit.
PS01124. HTH_ARAC_FAMILY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The araC gene of Escherichia coli: transcriptional and translational start-points and complete nucleotide sequence."
    Wallace R.G., Lee N., Fowler A.V.
    Gene 12:179-190(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B/R.
  2. "DNA sequence of the araC regulatory gene from Escherichia coli B/r."
    Miyada C.G., Horwitz A.H., Cass L.G., Timko J., Wilcox G.
    Nucleic Acids Res. 8:5267-5274(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B/R.
  3. "Is the amino acid but not the nucleotide sequence of the Escherichia coli araC gene conserved?"
    Stoner C.M., Schleif R.
    J. Mol. Biol. 154:649-652(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "The araC regulatory gene mRNA contains a leader sequence."
    Cass L.G., Horwitz A.H., Miyada C.G., Greenfield L., Wilcox G.
    Mol. Gen. Genet. 180:219-226(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
    Strain: B/R.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "The 1.6 A crystal structure of the AraC sugar-binding and dimerization domain complexed with D-fucose."
    Soisson S.M., Macdougall-Shackleton B., Schleif R., Wolberger C.
    J. Mol. Biol. 273:226-237(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-178.
  10. "Structural basis for ligand-regulated oligomerization of AraC."
    Soisson S.M., Macdougall-Shackleton B., Schleif R., Wolberger C.
    Science 276:421-425(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 AND 2.8 ANGSTROMS).

Entry informationi

Entry nameiARAC_ECOLI
AccessioniPrimary (citable) accession number: P0A9E0
Secondary accession number(s): P03021, Q47056
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 99 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.