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argR arginine repressor [ Mycobacterium tuberculosis H37Rv ]

Gene ID: 885091, updated on 6-Oct-2023
Gene symbol
argR
Gene description
arginine repressor
Locus tag
Rv1657
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Mycobacterium tuberculosis H37Rv (strain: H37Rv, type-material: type strain of Mycobacterium tuberculosis)
Lineage
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex
Also known as
ahrC
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Sequence:
NC_000962.3 (1870842..1871354)

NC_000962.3Genomic Context describing neighboring genes Neighboring gene N-acetyl-gamma-glutamyl-phoshate reductase Neighboring gene bifunctional glutamate N-acetyltransferase/amino-acid acetyltransferase Neighboring gene acetylglutamate kinase Neighboring gene acetylornithine aminotransferase Neighboring gene ornithine carbamoyltransferase Neighboring gene argininosuccinate synthase Neighboring gene argininosuccinate lyase

Genomic Sequence:
NC_000962.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Crystal structure of the intermediate complex of the arginine repressor from Mycobacterium tuberculosis bound with its DNA operator reveals detailed mechanism of arginine repression. Cherney LT, et al. J Mol Biol, 2010 Jun 4. PMID 20382162
  2. Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis. Cherney LT, et al. Acta Crystallogr D Biol Crystallogr, 2008 Sep. PMID 18703843, Free PMC Article
  3. Expression, purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis. Lu GJ, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007 Nov 1. PMID 18007044, Free PMC Article
  4. TubercuList--10 years after. Lew JM, et al. Tuberculosis (Edinb), 2011 Jan. PMID 20980199
  5. Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv. Camus JC, et al. Microbiology (Reading), 2002 Oct. PMID 12368430

See all (6) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The core trimers are rotated relative to one another as in the other holo hexamers of Mycobacterium tuberculosis ArgR, although the L-arginine ligands have only partial density and do not fully occupy the arginine-binding sites.
    Title: Crystal structure of the intermediate complex of the arginine repressor from Mycobacterium tuberculosis bound with its DNA operator reveals detailed mechanism of arginine repression.
  2. All residues in MtbCArgR deemed to be important for hexamer formation and for arginine binding have been identified from the experimentally determined structures presented.
    Title: Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis.
  3. The crystals belong to space group P1 and the Matthews coefficient suggests that the crystals contain six C-terminal domain molecules per unit cell.
    Title: Expression, purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis.
Submit: New GeneRIF Correction

Homology

Preferred Names
arginine repressor
NP_216173.1
  • Arginine repressor

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000962.3 Reference assembly

    Range
    1870842..1871354
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_216173.1 arginine repressor [Mycobacterium tuberculosis H37Rv]

    See identical proteins and their annotated locations for NP_216173.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    R4M5S9
    Conserved Domains (1) summary
    PRK03341
    Location:6 → 170
    PRK03341; arginine repressor; Provisional
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
3ERE_D.1
3FHZ_A.1
3FHZ_B.1
3FHZ_C.1
3FHZ_D.1
3FHZ_E.1
3FHZ_F.1
3LAJ_A.1
3LAJ_B.1
3LAJ_C.1
3LAJ_D.1
3LAJ_E.1
3LAJ_F.1
3LAP_A.1
3LAP_B.1
3LAP_C.1
3LAP_D.1
3LAP_E.1
3LAP_F.1
P9WPY9.1

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