Nitrogen regulation protein NR(I)

Details

Name
Nitrogen regulation protein NR(I)
Synonyms
  • ntrC
Gene Name
glnG
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0010893|Nitrogen regulation protein NR(I)
MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLAALASKTPDVLLSDIRMPGM
DGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIS
HYQEQQQPRNIEVNGPTTDMIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHA
LHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDE
IGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLERRVQEGKFREDLFHR
LNVIRIHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETETALTRLAWPGNVRQL
ENTCRWLTVMAAGQEVLIQDLPGELFEASTPDSPSHLPPDSWATLLAQWADRALRSGHQN
LLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME
Number of residues
469
Molecular Weight
52270.29
Theoretical pI
6.62
GO Classification
Functions
ATP binding / phosphorelay response regulator activity / sequence-specific DNA binding
Processes
nitrogen fixation / regulation of nitrogen utilization / regulation of transcription, DNA-templated / transcription, DNA-templated
Components
intracellular
General Function
Sequence-specific dna binding
Specific Function
Member of the two-component regulatory system NtrB/NtrC involved in the activation of nitrogen assimilatory genes such as GlnA. NtrC is phosphorylated by NtrB and interacts with sigma-54.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0010894|Nitrogen regulation protein NR(I) (glnG)
ATGCAACGAGGAATAGTCTGGGTCGTCGATGATGATAGTTCCATCCGTTGGGTGCTTGAG
CGTGCTCTCGCCGGGGCAGGGTTGACCTGTACCACCTTTGAGAATGGTAATGAAGTACTG
GCTGCGCTGGCCAGTAAAACGCCGGACGTCTTGCTGTCGGATATCCGAATGCCGGGAATG
GACGGGCTGGCGCTATTAAAGCAGATTAAACAGCGTCACCCGATGCTTCCGGTCATCATT
ATGACCGCGCATTCCGATTTAGATGCCGCCGTGAGCGCCTATCAGCAGGGGGCGTTTGAT
TATCTGCCTAAACCGTTTGATATTGATGAAGCCGTCGCTCTGGTCGAGCGCGCGATTAGC
CACTATCAGGAGCAGCAACAGCCGCGTAATATCGAGGTTAACGGCCCGACAACAGACATG
ATAGGCGAAGCGCCCGCCATGCAGGATGTGTTTCGCATTATTGGTCGGCTGTCGCGTTCT
TCGATTAGCGTGCTGATTAACGGCGAATCAGGGACCGGTAAAGAACTGGTCGCCCATGCG
CTTCACCGCCATAGCCCACGCGCCAAAGCGCCGTTTATCGCACTCAATATGGCGGCCATC
CCGAAAGATTTGATTGAATCCGAACTGTTTGGCCATGAGAAAGGCGCTTTTACCGGGGCG
AATACCATCCGGCAGGGCCGTTTCGAGCAGGCTGACGGCGGCACGCTGTTTCTGGACGAA
ATTGGCGATATGCCGCTGGATGTCCAGACTCGTCTGTTACGCGTGCTGGCTGACGGACAG
TTCTACCGCGTGGGCGGGTACGCGCCGGTAAAAGTCGATGTGCGCATTATCGCCGCCACC
CACCAGAACCTCGAACGACGCGTTCAGGAAGGGAAATTCCGCGAAGACCTGTTCCACCGC
CTGAACGTGATTCGTATCCATCTTCCGCCGTTGCGTGAACGCCGTGAGGATATTCCGCGC
CTGGCGCGCCATTTTTTGCAGGTCGCCGCCCGTGAATTAGGCGTGGAAGCCAAATTATTA
CATCCGGAAACCGAAACGGCGTTAACGCGCCTGGCATGGCCTGGTAACGTGCGTCAGTTA
GAAAATACCTGCCGCTGGCTCACCGTCATGGCCGCCGGACAGGAGGTATTGATCCAGGAT
TTACCGGGCGAACTGTTTGAAGCCTCGACGCCGGATAGCCCGTCCCACCTGCCGCCGGAT
AGCTGGGCTACATTACTGGCACAATGGGCGGACCGCGCCTTGCGATCCGGTCATCAAAAC
CTGCTTTCTGAAGCGCAGCCAGAACTGGAGAGAACGCTACTGACCACGGCATTACGCCAT
ACGCAGGGTCATAAACAGGAAGCCGCCAGGCTGCTCGGTTGGGGGCGAAACACCCTAACG
CGGAAGTTGAAAGAGCTGGGAATGGAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP41789
UniProtKB Entry NameNTRC_SALTY
GenBank Protein ID728724
GenBank Gene IDX85104
General References
  1. Flashner Y, Weiss DS, Keener J, Kustu S: Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain. J Mol Biol. 1995 Jun 16;249(4):700-13. [Article]
  2. McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, Porwollik S, Ali J, Dante M, Du F, Hou S, Layman D, Leonard S, Nguyen C, Scott K, Holmes A, Grewal N, Mulvaney E, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
  3. Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE: Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry. 1995 Jan 31;34(4):1413-24. [Article]
  4. Pelton JG, Kustu S, Wemmer DE: Solution structure of the DNA-binding domain of NtrC with three alanine substitutions. J Mol Biol. 1999 Oct 8;292(5):1095-110. [Article]
  5. Kern D, Volkman BF, Luginbuhl P, Nohaile MJ, Kustu S, Wemmer DE: Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature. 1999 Dec 23-30;402(6764):894-8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01857PhosphoaspartateexperimentalunknownDetails