RegulonDB RegulonDB 10.10: Gene Form
   

glnB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

glrR hmp glnB qseG PurR glnBp3 glnBp3 glnBp2 glnBp2 glnBp1 glnBp1

Gene      
Name: glnB    Texpresso search in the literature
Synonym(s): ECK2550, EG10384, b2553
Genome position(nucleotides): 2687070 <-- 2687408 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
51.03
External database links:  
ASAP:
ABE-0008398
CGSC:
32933
ECHOBASE:
EB0379
ECOLIHUB:
glnB
OU-MICROARRAY:
b2553
STRING:
511145.b2553
COLOMBOS: glnB


Product      
Name: nitrogen regulatory protein PII-1
Synonym(s): GlnB, PII, PII-1, [protein PII], regulatory protein P-II, regulation of nitrogen metabolism and fatty acid biosynthesis, unmodified PII
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 12.425
Isoelectric point: 4.952
Motif(s):
 
Type Positions Sequence
2 -> 8 KKIDAII
27 -> 36 GMTVTEVKGF
83 -> 83 T
97 -> 102 ARVIRI
40 -> 40 K

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.1 - amino acids --> 1.5.1.2 - glutamine
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.4 - fatty acids and phosphatidic acid
  1 - metabolism --> 1.8 - metabolism of other compounds --> 1.8.3 - nitrogen metabolism
  3 - regulation --> 3.1 - type of regulation --> 3.1.3 - posttranscriptional --> 3.1.3.3 - inhibition / activation of enzymes
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
molecular_function GO:0005515 - protein binding
GO:0008047 - enzyme activator activity
GO:0030234 - enzyme regulator activity
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0042802 - identical protein binding
GO:0036094 - small molecule binding
biological_process GO:0050790 - regulation of catalytic activity
GO:0006808 - regulation of nitrogen utilization
GO:0042304 - regulation of fatty acid biosynthetic process
Evidence: [APPHINH] Assay of protein purified to homogeneity from its native host
[IMP] Inferred from mutant phenotype
Reference(s): [1] Atkinson MR., et al., 1994
[2] Gerhardt EC., et al., 2015
[3] Jiang P., et al., 1999
[4] Jiang P., et al., 1997
External database links:  
DIP:
DIP-35005N
ECOCYC:
PROTEIN-PII
ECOLIWIKI:
b2553
INTERPRO:
IPR002332
INTERPRO:
IPR017918
INTERPRO:
IPR015867
INTERPRO:
IPR011322
INTERPRO:
IPR002187
MODBASE:
P0A9Z1
PANTHER:
PTHR30115
PDB:
1PIL
PDB:
2PII
PDB:
5L9N
PFAM:
PF00543
PRIDE:
P0A9Z1
PRINTS:
PR00340
PRODB:
PRO_000022783
PROSITE:
PS00638
PROSITE:
PS51343
PROSITE:
PS00496
REFSEQ:
NP_417048
SMART:
SM00938
SMR:
P0A9Z1
UNIPROT:
P0A9Z1


Operon      
Name: glrR-glnB         
Operon arrangement:
Transcription unit        Promoter
glnB
glnB
glnB
glrR-glnB
yfhA


Transcriptional Regulation      
Display Regulation             
Repressed by: PurR


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References


Reference(s)    

 [1] Atkinson MR., Kamberov ES., Weiss RL., Ninfa AJ., 1994, Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC)., J Biol Chem 269(45):28288-93

 [2] Gerhardt EC., Rodrigues TE., Muller-Santos M., Pedrosa FO., Souza EM., Forchhammer K., Huergo LF., 2015, The bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl-CoA carboxylase., Mol Microbiol 95(6):1025-35

 [3] Jiang P., Ninfa AJ., 1999, Regulation of autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein., J Bacteriol 181(6):1906-11

 [4] Jiang P., Zucker P., Atkinson MR., Kamberov ES., Tirasophon W., Chandran P., Schefke BR., Ninfa AJ., 1997, Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors., J Bacteriol 179(13):4342-53


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