Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei212 – 2121Glyoxylate
Binding sitei222 – 2221Glyoxylate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi46 – 6520H-T-H motifPROSITE-ProRule annotationAdd
BLAST

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.
RETL1328306-WGS:GSTH-5075-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi143 – 1431L → D: Strongly reduced promoter binding and tetramerization. 1 Publication
Mutagenesisi146 – 1461M → D: Strongly reduced promoter binding and tetramerization. 1 Publication
Mutagenesisi154 – 1541L → D: Strongly reduced promoter binding and tetramerization. 1 Publication
Mutagenesisi220 – 2201L → D: Loss of promoter binding and tetramerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Acetate operon repressorPRO_0000201758Add
BLAST

Proteomic databases

EPDiP16528.
PaxDbiP16528.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

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

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi99 – 11618Combined sources
Beta strandi118 – 1269Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi156 – 1594Combined sources
Helixi160 – 1667Combined sources
Helixi171 – 1755Combined sources
Helixi177 – 1804Combined sources
Helixi194 – 20714Combined sources
Beta strandi209 – 2179Combined sources
Beta strandi220 – 2289Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 24310Combined sources
Turni244 – 2463Combined sources
Helixi249 – 2513Combined sources
Helixi252 – 27322Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 24-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16528.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 8663HTH iclR-typePROSITE-ProRule annotationAdd
BLAST
Domaini101 – 272172IclR-EDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 1612Glyoxylate binding
Regioni239 – 2413Glyoxylate binding

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.
OrthoDBiEOG6MWN8D.
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 AAA50561.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC43112.1 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
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. Positions 24-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiP16528.
PaxDbiP16528.

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.
OrthoDBiEOG6MWN8D.
PhylomeDBiP16528.

Enzyme and pathway databases

BioCyciEcoCyc:PD04099.
ECOL316407:JW3978-MONOMER.
RETL1328306-WGS:GSTH-5075-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...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of the glyoxylate bypass operon: cloning and characterization of iclR."
    Sunnarborg A., Klumpp D.J., Chung T., Laporte D.C.
    J. Bacteriol. 172:2642-2649(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Overproduction and characterization of the iclR gene product of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2."
    Negre D., Cortay J.-C., Old I.G., Galinier A., Richaud C., Saint-Girons I., Cozzone A.J.
    Gene 97:29-37(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Primary structure of the intergenic region between aceK and iclR in the Escherichia coli chromosome."
    Galinier A., Bleicher F., Negre D., Perriere G., Duclos B., Cozzone A.J., Cortay J.-C.
    Gene 97:149-150(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-274.
  7. "Glyoxylate and pyruvate are antagonistic effectors of the Escherichia coli IclR transcriptional regulator."
    Lorca G.L., Ezersky A., Lunin V.V., Walker J.R., Altamentova S., Evdokimova E., Vedadi M., Bochkarev A., Savchenko A.
    J. Biol. Chem. 282:16476-16491(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 98-274 IN COMPLEXES WITH PYRUVATE AND GLYOXYLATE, SUBUNIT, MUTAGENESIS OF LEU-143; MET-146; LEU-154 AND LEU-220.
  8. "Crystal structure analysis of the E. coli glyoxylate regulatory protein ligand binding domain."
    Walker J.R., Skarina T., Kudrytska M., Arrowsmith C., Edwards A., Savchenko A.
    Submitted (JAN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 98-274.

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: May 11, 2016
This is version 146 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.