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Protein

Acetate operon repressor

Gene

iclR

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

Functioni

Regulation of the glyoxylate bypass operon (aceBAK), which encodes isocitrate lyase, malate synthase as well as isocitrate dehydrogenase kinase/phosphorylase. Glyoxylate disrupts the interaction with the promoter by favoring the inactive dimeric form. Pyruvate enhances promoter binding by stabilizing the tetrameric form.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei212Glyoxylate1
Binding sitei222Glyoxylate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi46 – 65H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Glyoxylate bypass, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD04099.
ECOL316407:JW3978-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetate operon repressor
Gene namesi
Name:iclR
Ordered Locus Names:b4018, JW3978
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10491. iclR.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi143L → D: Strongly reduced promoter binding and tetramerization. 1 Publication1
Mutagenesisi146M → D: Strongly reduced promoter binding and tetramerization. 1 Publication1
Mutagenesisi154L → D: Strongly reduced promoter binding and tetramerization. 1 Publication1
Mutagenesisi220L → D: Loss of promoter binding and tetramerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002017581 – 274Acetate operon repressorAdd BLAST274

Proteomic databases

EPDiP16528.
PaxDbiP16528.
PRIDEiP16528.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4263460. 10 interactors.
DIPiDIP-10008N.
IntActiP16528. 17 interactors.
MINTiMINT-1226737.
STRINGi511145.b4018.

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi99 – 116Combined sources18
Beta strandi118 – 126Combined sources9
Turni127 – 130Combined sources4
Beta strandi131 – 138Combined sources8
Beta strandi143 – 146Combined sources4
Beta strandi156 – 159Combined sources4
Helixi160 – 166Combined sources7
Helixi171 – 175Combined sources5
Helixi177 – 180Combined sources4
Helixi194 – 207Combined sources14
Beta strandi209 – 217Combined sources9
Beta strandi220 – 228Combined sources9
Beta strandi230 – 232Combined sources3
Beta strandi234 – 243Combined sources10
Turni244 – 246Combined sources3
Helixi249 – 251Combined sources3
Helixi252 – 273Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TD5X-ray2.30A/B/C/D98-274[»]
2O99X-ray1.70A/B/C/D98-274[»]
2O9AX-ray1.80A/B/C/D98-274[»]
ProteinModelPortaliP16528.
SMRiP16528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16528.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 86HTH iclR-typePROSITE-ProRule annotationAdd BLAST63
Domaini101 – 272IclR-EDPROSITE-ProRule annotationAdd BLAST172

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni160 – 161Glyoxylate binding2
Regioni239 – 241Glyoxylate binding3

Sequence similaritiesi

Contains 1 HTH iclR-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 iclR-ED (iclR effector binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG41069M3. Bacteria.
COG1414. LUCA.
HOGENOMiHOG000107041.
InParanoidiP16528.
KOiK13641.
OMAiIAACIFD.
PhylomeDBiP16528.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.450.40. 1 hit.
InterProiIPR029016. GAF_dom-like.
IPR014757. Tscrpt_reg_IclR_C.
IPR005471. Tscrpt_reg_IclR_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF09339. HTH_IclR. 1 hit.
PF01614. IclR. 1 hit.
[Graphical view]
SMARTiSM00346. HTH_ICLR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55781. SSF55781. 1 hit.
PROSITEiPS51077. HTH_ICLR. 1 hit.
PS51078. ICLR_ED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAPIPAKRG RKPAVATAPA TGQVQSLTRG LKLLEWIAES NGSVALTELA
60 70 80 90 100
QQAGLPNSTT HRLLTTMQQQ GFVRQVGELG HWAIGAHAFM VGSSFLQSRN
110 120 130 140 150
LLAIVHPILR NLMEESGETV NMAVLDQSDH EAIIIDQVQC THLMRMSAPI
160 170 180 190 200
GGKLPMHASG AGKAFLAQLS EEQVTKLLHR KGLHAYTHAT LVSPVHLKED
210 220 230 240 250
LAQTRKRGYS FDDEEHALGL RCLAACIFDE HREPFAAISI SGPISRITDD
260 270
RVTEFGAMVI KAAKEVTLAY GGMR
Length:274
Mass (Da):29,739
Last modified:August 1, 1990 - v1
Checksum:i7C8A7E9FD2841D0C
GO

Sequence cautioni

The sequence AAA50561 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC43112 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31761 Genomic DNA. Translation: AAA24008.1.
M63914 Genomic DNA. Translation: AAA50561.1. Different initiation.
U00006 Genomic DNA. Translation: AAC43112.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76988.2.
AP009048 Genomic DNA. Translation: BAE78020.1.
M63497 Genomic DNA. Translation: AAA73003.1.
RefSeqiNP_418442.2. NC_000913.3.
WP_000226403.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76988; AAC76988; b4018.
BAE78020; BAE78020; BAE78020.
GeneIDi948524.
KEGGiecj:JW3978.
eco:b4018.
PATRICi32123565. VBIEscCol129921_4131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31761 Genomic DNA. Translation: AAA24008.1.
M63914 Genomic DNA. Translation: AAA50561.1. Different initiation.
U00006 Genomic DNA. Translation: AAC43112.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76988.2.
AP009048 Genomic DNA. Translation: BAE78020.1.
M63497 Genomic DNA. Translation: AAA73003.1.
RefSeqiNP_418442.2. NC_000913.3.
WP_000226403.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TD5X-ray2.30A/B/C/D98-274[»]
2O99X-ray1.70A/B/C/D98-274[»]
2O9AX-ray1.80A/B/C/D98-274[»]
ProteinModelPortaliP16528.
SMRiP16528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263460. 10 interactors.
DIPiDIP-10008N.
IntActiP16528. 17 interactors.
MINTiMINT-1226737.
STRINGi511145.b4018.

Proteomic databases

EPDiP16528.
PaxDbiP16528.
PRIDEiP16528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76988; AAC76988; b4018.
BAE78020; BAE78020; BAE78020.
GeneIDi948524.
KEGGiecj:JW3978.
eco:b4018.
PATRICi32123565. VBIEscCol129921_4131.

Organism-specific databases

EchoBASEiEB0486.
EcoGeneiEG10491. iclR.

Phylogenomic databases

eggNOGiENOG41069M3. Bacteria.
COG1414. LUCA.
HOGENOMiHOG000107041.
InParanoidiP16528.
KOiK13641.
OMAiIAACIFD.
PhylomeDBiP16528.

Enzyme and pathway databases

BioCyciEcoCyc:PD04099.
ECOL316407:JW3978-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP16528.
PROiP16528.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.450.40. 1 hit.
InterProiIPR029016. GAF_dom-like.
IPR014757. Tscrpt_reg_IclR_C.
IPR005471. Tscrpt_reg_IclR_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF09339. HTH_IclR. 1 hit.
PF01614. IclR. 1 hit.
[Graphical view]
SMARTiSM00346. HTH_ICLR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55781. SSF55781. 1 hit.
PROSITEiPS51077. HTH_ICLR. 1 hit.
PS51078. ICLR_ED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiICLR_ECOLI
AccessioniPrimary (citable) accession number: P16528
Secondary accession number(s): P76782, Q2M6T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Glyoxylate and pyruvate occupy the same site.

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.