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glnD glnD glnB glnB glnK glnK ampM ampM glnE glnE glnR glnR dapD dapD aspB aspB glnA glnA glnF glnF rpsA rpsA
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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textmining
co-expression
protein homology
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glnD[protein-PII] uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. (912 aa)    
Predicted Functional Partners:
glnB
Similar to Escherichia coli hypothetical protein YhfZ SW:YHFZ_ECOLI (P45552) (273 aa) fasta scores: E(): 0,52.0% id in 273 aa, and to Bacillus halodurans hypothetical protein BH0586 TR:Q9KF99 (EMBL:AP001509) (306 aa) fasta scores: E(): 1.9e-29, 34.9% id in 307 aa. Possible alternative translational start sites. Contains a frameshift after codon 189. Frame shift occurs at a poly A decamer. The sequence has been checked and is believed to be correct.
 
 
 0.996
glnK
Similar to Escherichia coli nitrogen regulatory protein P-II GlnK SW:GLNK_ECOLI (P38504) (112 aa) fasta scores: E(): 0, 94.6% id in 112 aa, and to Klebsiella pneumoniae PII-like nitrogen regulatory protein GlnK TR:Q9ZA65 (EMBL:AJ006531) (112 aa) fasta scores: E(): 0,95.5% id in 112 aa; Belongs to the P(II) protein family.
 
 
 0.931
ampM
Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
  
    0.815
glnE
Glutamate-ammonia-ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...]
 
  
 0.803
glnR
Two component regulatory protein involved in nitrogen assimilation; Similar to Escherichia coli nitrogen regulation protein NtrB SW:NTRB_ECOLI (P06712) (349 aa) fasta scores: E(): 0, 86.5% id in 349 aa.
  
 
 
 0.802
dapD
Similar to Escherichia coli 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase dapD SW:DAPD_ECOLI (P03948) (274 aa) fasta scores: E(): 0, 92.3% id in 274 aa, and to Mycobacterium bovis 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase dapD SW:DAPD_MYCBO (P56220) (274 aa) fasta scores: E(): 0, 93.8% id in 274 aa; Belongs to the transferase hexapeptide repeat family.
     
 0.615
aspB
Similar to Escherichia coli glutamate synthase [NADPH] large chain precursor GltB or AspB SW:GLTB_ECOLI (P09831) (1517 aa) fasta scores: E(): 0, 87.4% id in 1497 aa, and to Vibrio cholerae glutamate synthase, large subunit Vc2376 TR:Q9KPJ1 (EMBL:AE004308) (1487 aa) fasta scores: E(): 0, 73.7% id in 1488 aa.
  
  
 0.608
glnA
Glutamine synthetase; Highly similar to Escherichia coli glutamine synthetase GlnA SW:GLNA_ECOLI (P06711) (468 aa) fasta scores: E(): 0, 91.5% id in 468 aa.
 
  
 0.549
glnF
RNA polymerase sigma-54 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
  
   
 0.546
rpsA
30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
  
  
 0.530
Your Current Organism:
Yersinia pestis
NCBI taxonomy Id: 214092
Other names: Y. pestis CO92, Yersinia pestis CO92, Yersinia pestis str. CO92, Yersinia pestis strain CO92
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