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Protein

HTH-type transcriptional repressor AllR

Gene

allR

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

Functioni

Negative regulator of allantoin and glyoxylate utilization operons. Binds to the gcl promoter and to the allS-allA intergenic region. Binding to DNA is abolished by glyoxylate.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei207Glyoxylate1
Binding sitei217Glyoxylate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi43 – 62H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

  • DNA binding Source: GO_Central
  • DNA binding transcription factor activity Source: EcoCyc
  • identical protein binding Source: IntAct

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:G6276-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional repressor AllR
Alternative name(s):
Negative regulator of allantoin and glyoxylate utilization operons
Gene namesi
Name:allR
Synonyms:glxA3, ybbU
Ordered Locus Names:b0506, JW0494
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13616 allR

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi135 – 142CKSMVRMC → APA: Loss of repressor activity. Loss of DNA binding. Reduces assembly into functionally active tetramers. 1 Publication8
Mutagenesisi141M → A: No effect on repressor activity. Loss of glyoxylate-triggered dissociation from DNA. 1 Publication1
Mutagenesisi142C → W: Strongly reduced repressor activity. Reduces DNA binding. Prevents assembly into functionally active tetramers. 1 Publication1
Mutagenesisi215L → A: Reduced repressor activity. Loss of glyoxylate-triggered dissociation from DNA. 1 Publication1
Mutagenesisi217C → A or S: Slightly reduced repressor activity. Loss of glyoxylate-triggered dissociation from DNA. 1 Publication1
Mutagenesisi234S → A or N: Reduced repressor activity. Loss of glyoxylate-triggered dissociation from DNA. 1 Publication1
Mutagenesisi236S → A or M: Slightly reduced repressor activity. Loss of glyoxylate-triggered dissociation from DNA. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002017531 – 271HTH-type transcriptional repressor AllRAdd BLAST271

Proteomic databases

PaxDbiP0ACN4
PRIDEiP0ACN4

Interactioni

Subunit structurei

Homotetramer and homodimer. Homotetramer in its active, DNA-bound form. Homodimer in its inactive form.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259871, 7 interactors
DIPiDIP-47907N
IntActiP0ACN4, 21 interactors
STRINGi316385.ECDH10B_0462

Structurei

Secondary structure

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi97 – 113Combined sources17
Beta strandi115 – 123Combined sources9
Beta strandi126 – 133Combined sources8
Beta strandi138 – 141Combined sources4
Beta strandi148 – 150Combined sources3
Turni151 – 153Combined sources3
Helixi155 – 161Combined sources7
Helixi166 – 176Combined sources11
Helixi189 – 202Combined sources14
Beta strandi205 – 212Combined sources8
Beta strandi215 – 223Combined sources9
Beta strandi229 – 238Combined sources10
Turni239 – 241Combined sources3
Helixi244 – 246Combined sources3
Helixi247 – 265Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TF1X-ray1.80A/B/C/D97-271[»]
ProteinModelPortaliP0ACN4
SMRiP0ACN4
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACN4

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 83HTH iclR-typePROSITE-ProRule annotationAdd BLAST63
Domaini98 – 267IclR-EDPROSITE-ProRule annotationAdd BLAST170

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni154 – 156Glyoxylate binding3
Regioni234 – 236Glyoxylate binding3

Phylogenomic databases

eggNOGiENOG4108N16 Bacteria
COG1414 LUCA
HOGENOMiHOG000107041
InParanoidiP0ACN4
KOiK10973
OMAiHEESINC
PhylomeDBiP0ACN4

Family and domain databases

Gene3Di1.10.10.10, 1 hit
3.30.450.40, 1 hit
InterProiView protein in InterPro
IPR029016 GAF-like_dom_sf
IPR014757 Tscrpt_reg_IclR_C
IPR005471 Tscrpt_reg_IclR_N
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF09339 HTH_IclR, 1 hit
PF01614 IclR, 1 hit
SMARTiView protein in SMART
SM00346 HTH_ICLR, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS51077 HTH_ICLR, 1 hit
PS51078 ICLR_ED, 1 hit

Sequencei

Sequence statusi: Complete.

P0ACN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEVRRRGRP GQAEPVAQKG AQALERGIAI LQYLEKSGGS SSVSDISLNL
60 70 80 90 100
DLPLSTTFRL LKVLQAADFV YQDSQLGWWH IGLGVFNVGA AYIHNRDVLS
110 120 130 140 150
VAGPFMRRLM LLSGETVNVA IRNGNEAVLI GQLECKSMVR MCAPLGSRLP
160 170 180 190 200
LHASGAGKAL LYPLAEEELM SIILQTGLQQ FTPTTLVDMP TLLKDLEQAR
210 220 230 240 250
ELGYTVDKEE HVVGLNCIAS AIYDDVGSVV AAISISGPSS RLTEDRFVSQ
260 270
GELVRDTARD ISTALGLKAH P
Length:271
Mass (Da):29,270
Last modified:November 22, 2005 - v1
Checksum:i476F59EEC0F8308B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89024 Genomic DNA Translation: AAB93847.1
U82664 Genomic DNA Translation: AAB40259.1
U00096 Genomic DNA Translation: AAC73608.1
AP009048 Genomic DNA Translation: BAE76284.1
PIRiA64782
RefSeqiNP_415039.1, NC_000913.3
WP_000141275.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73608; AAC73608; b0506
BAE76284; BAE76284; BAE76284
GeneIDi945333
KEGGiecj:JW0494
eco:b0506
PATRICifig|1411691.4.peg.1771

Entry informationi

Entry nameiALLR_ECOLI
AccessioniPrimary (citable) accession number: P0ACN4
Secondary accession number(s): P77734, Q2MBS2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: March 28, 2018
This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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