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STRINGSTRING
STRING protein interaction network
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.
Node Color
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
KFX07355.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (233 aa)    
Predicted Functional Partners:
tsaD
UGMP family protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction; Belongs to the KAE1 / TsaD family.
 
 0.989
KFX05135.1
ADP-binding protein; Needed for nucleoid integrity; possibly involved in cell wall synthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.987
birA
biotin--[acetyl-CoA-carboxylase] synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
 
    0.943
ribD
5-amino-6-(5-phosphoribosylamino)uracil reductase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
    
  0.800
tsaC
tRNA(ANN) t(6)A37 threonylcarbamoyladenosine modification protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
 
  
 0.782
alr
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
 
  
 0.739
KFX07433.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SUA5 family.
    
 0.691
tadA
tRNA adenosine deaminase; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family.
 
  
 0.661
rimI
Ribosomal-protein-alanine acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S18.
 
 0.640
tilS
tRNA(Ile)-lysidine ligase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family.
 
   
 0.613
Your Current Organism:
Pectobacterium betavasculorum
NCBI taxonomy Id: 55207
Other names: ATCC 43762, CFBP 2122, CIP 105193, DSM 18076, Erwinia carotovora subsp. betavasculorum, ICMP 4226, LMG 2464, LMG 2466, LMG:2464, LMG:2466, NCPPB 2795, P. betavasculorum, Pectobacterium carotovorum subsp. betavasculorum, UCPB 193
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