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Protein

HTH-type transcriptional repressor AcnR

Gene

acnR

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

AcnR negatively controls the expression of the aconitase gene acn. Binds to the imperfect inverted repeat in the acn promoter region.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei130Citrate1 Publication1
Binding sitei134Citrate1 Publication1
Metal bindingi181Magnesium1 Publication1
Binding sitei185Citrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi33 – 52H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB

GO - Biological processi

  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciCORYNE:G18NG-11126-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional repressor AcnR1 Publication
Alternative name(s):
TetR-type regulator AcnR1 Publication
Gene namesi
Name:acnR1 Publication
Ordered Locus Names:Cgl1541, cg1738
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Deletion of acnR leads to a 5-fold increase of the aconitase activity. Overexpression of acnR leads to a 2-fold decrease of the aconitase activity.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43K → A: DNA binding affinity is almost completely abolished. Still forms a dimer. 1 Publication1
Mutagenesisi55K → A: DNA binding affinity is almost completely abolished. Still forms a dimer but the ratio of aggregated to dimeric protein is significantly higher. 1 Publication1
Mutagenesisi65E → A: No effect on DNA binding. 1 Publication1
Mutagenesisi66D → A: No effect on DNA binding. 1 Publication1
Mutagenesisi99R → A: Weaker binding to DNA. 1 Publication1
Mutagenesisi104K → A: DNA binding affinity is slightly reduced. Still forms a dimer but the ratio of aggregated to dimeric protein is significantly higher. 1 Publication1
Mutagenesisi109D → A: No effect on DNA binding. 1 Publication1
Mutagenesisi141R → A: No effect on DNA binding. 1 Publication1
Mutagenesisi143D → A: No effect on DNA binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000705711 – 188HTH-type transcriptional repressor AcnRAdd BLAST188

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi196627.cg1738.

Structurei

Secondary structure

1188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 31Combined sources20
Helixi34 – 41Combined sources8
Helixi45 – 52Combined sources8
Helixi55 – 88Combined sources34
Helixi90 – 92Combined sources3
Helixi93 – 101Combined sources9
Helixi103 – 108Combined sources6
Helixi110 – 119Combined sources10
Helixi121 – 136Combined sources16
Beta strandi142 – 144Combined sources3
Helixi146 – 165Combined sources20
Helixi173 – 184Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AC6X-ray2.54A2-188[»]
4ACIX-ray1.65A/B2-188[»]
4AF5X-ray1.90A1-188[»]
ProteinModelPortaliQ8NQ97.
SMRiQ8NQ97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 70HTH tetR-typePROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni79 – 80Citrate binding1 Publication2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IG5. Bacteria.
COG1309. LUCA.
HOGENOMiHOG000248228.
OMAiQSATRND.

Family and domain databases

Gene3Di1.10.357.10. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
[Graphical view]
PfamiPF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF48498. SSF48498. 1 hit.
PROSITEiPS50977. HTH_TETR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NQ97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVAAGDKPT NSRQEILEGA RRCFAEHGYE GATVRRLEEA TGKSRGAIFH
60 70 80 90 100
HFGDKENLFL ALAREDAARM AEVVSENGLV EVMRGMLEDP ERYDWMSVRL
110 120 130 140 150
EISKQLRTDP VFRAKWIDHQ SVLDEAVRVR LSRNVDKGQM RTDVPIEVLH
160 170 180
TFLETVLDGF ISRLATGAST EGLSEVLDLV EGTVRKRD
Length:188
Mass (Da):21,185
Last modified:October 1, 2002 - v1
Checksum:i54F31FA9A184B836
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB98934.1.
BX927152 Genomic DNA. Translation: CAF21549.1.
RefSeqiNP_600756.1. NC_003450.3.
WP_003856101.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB98934; BAB98934; BAB98934.
CAF21549; CAF21549; cg1738.
GeneIDi1019513.
KEGGicgb:cg1738.
cgl:NCgl1483.
PATRICi21495129. VBICorGlu203724_1508.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB98934.1.
BX927152 Genomic DNA. Translation: CAF21549.1.
RefSeqiNP_600756.1. NC_003450.3.
WP_003856101.1. NC_006958.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AC6X-ray2.54A2-188[»]
4ACIX-ray1.65A/B2-188[»]
4AF5X-ray1.90A1-188[»]
ProteinModelPortaliQ8NQ97.
SMRiQ8NQ97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg1738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB98934; BAB98934; BAB98934.
CAF21549; CAF21549; cg1738.
GeneIDi1019513.
KEGGicgb:cg1738.
cgl:NCgl1483.
PATRICi21495129. VBICorGlu203724_1508.

Phylogenomic databases

eggNOGiENOG4108IG5. Bacteria.
COG1309. LUCA.
HOGENOMiHOG000248228.
OMAiQSATRND.

Enzyme and pathway databases

BioCyciCORYNE:G18NG-11126-MONOMER.

Family and domain databases

Gene3Di1.10.357.10. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
[Graphical view]
PfamiPF00440. TetR_N. 1 hit.
[Graphical view]
PRINTSiPR00455. HTHTETR.
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF48498. SSF48498. 1 hit.
PROSITEiPS50977. HTH_TETR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACNR_CORGL
AccessioniPrimary (citable) accession number: Q8NQ97
Secondary accession number(s): Q6M549
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 86 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.