Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Co-expression
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[Homology]
Score
rimIRibosomal-protein-alanine acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S18. (147 aa)    
Predicted Functional Partners:
argA
Amino-acid N-acetyltransferase; [E] COG0548 Acetylglutamate kinase; Belongs to the acetyltransferase family. ArgA subfamily.
  
 
 0.897
KB13_1038
Peptidase M22, glycoprotease; [O] COG1214 Inactive homolog of metal-dependent proteases, putative molecular chaperone.
 
  
 0.871
KB13_380
Helicase c2; [KL] COG1199 Rad3-related DNA helicases.
       0.791
proS
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]
       0.791
KB13_1213
SelT/SelW/selH; [O] COG3526 Uncharacterized protein conserved in bacteria.
       0.773
KB13_789
Hypothetical protein.
       0.773
ectA
L-2,4-diaminobutyric acid acetyltransferase; Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
  
 
 0.673
ectB
Diaminobutyrate--2-oxoglutarate aminotransferase; Catalyzes reversively the conversion of L-aspartate beta- semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination with L-glutamate; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
    
 0.666
nadE
NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
    
  0.586
KB13_1045
[E] COG0160 4-aminobutyrate aminotransferase and related aminotransferases.
    
 0.577
Your Current Organism:
beta proteobacterium KB13
NCBI taxonomy Id: 314607
Other names: b. proteobacterium KB13
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