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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301Citrate1 Publication
Binding sitei134 – 1341Citrate1 Publication
Metal bindingi181 – 1811Magnesium1 Publication
Binding sitei185 – 1851Citrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi33 – 5220H-T-H motifPROSITE-ProRule annotationAdd
BLAST

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

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
ProteomesiUP000000582 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431K → A: DNA binding affinity is almost completely abolished. Still forms a dimer. 1 Publication
Mutagenesisi55 – 551K → A: DNA binding affinity is almost completely abolished. Still forms a dimer but the ratio of aggregated to dimeric protein is significantly higher. 1 Publication
Mutagenesisi65 – 651E → A: No effect on DNA binding. 1 Publication
Mutagenesisi66 – 661D → A: No effect on DNA binding. 1 Publication
Mutagenesisi99 – 991R → A: Weaker binding to DNA. 1 Publication
Mutagenesisi104 – 1041K → A: DNA binding affinity is slightly reduced. Still forms a dimer but the ratio of aggregated to dimeric protein is significantly higher. 1 Publication
Mutagenesisi109 – 1091D → A: No effect on DNA binding. 1 Publication
Mutagenesisi141 – 1411R → A: No effect on DNA binding. 1 Publication
Mutagenesisi143 – 1431D → A: No effect on DNA binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188HTH-type transcriptional repressor AcnRPRO_0000070571Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi196627.cg1738.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 3120Combined sources
Helixi34 – 418Combined sources
Helixi45 – 528Combined sources
Helixi55 – 8834Combined sources
Helixi90 – 923Combined sources
Helixi93 – 1019Combined sources
Helixi103 – 1086Combined sources
Helixi110 – 11910Combined sources
Helixi121 – 13616Combined sources
Beta strandi142 – 1443Combined sources
Helixi146 – 16520Combined sources
Helixi173 – 18412Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 7061HTH tetR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 802Citrate binding1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1309.
HOGENOMiHOG000248228.
OMAiQGLVQVM.
OrthoDBiEOG6ZKXQV.

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.
YP_225825.1. 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.
YP_225825.1. NC_006958.1.

3D structure databases

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

eggNOGiCOG1309.
HOGENOMiHOG000248228.
OMAiQGLVQVM.
OrthoDBiEOG6ZKXQV.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  3. "Identification of AcnR, a TetR-type repressor of the aconitase gene acn in Corynebacterium glutamicum."
    Krug A., Wendisch V.F., Bott M.
    J. Biol. Chem. 280:585-595(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT.
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  4. "Crystal and solution studies reveal that the transcriptional regulator AcnR of Corynebacterium glutamicum is regulated by citrate-Mg2+ binding to a non-canonical pocket."
    Garcia-Nafria J., Baumgart M., Turkenburg J.P., Wilkinson A.J., Bott M., Wilson K.S.
    J. Biol. Chem. 288:15800-15812(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-188 IN COMPLEX WITH CITRATE AND MAGNESIUM, FUNCTION, MUTAGENESIS OF LYS-43; LYS-55; GLU-65; ASP-66; ARG-99; LYS-104; ARG-141 AND ASP-143, SUBUNIT.

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: June 24, 2015
This is version 82 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

External Data

Dasty 3

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 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.