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
VC_2512Conserved hypothetical protein; Identified by Glimmer2; putative. (129 aa)    
Predicted Functional Partners:
pta
Phosphate acetyltransferase; Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ family.
   
 0.813
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
  
 
 0.804
VC_0705
Chorismate mutase/prephenate dehydratase; Similar to GB:L42023 SP:P43900 PID:1006481 PID:1221267 PID:1205390; identified by sequence similarity; putative.
    
 0.781
VC_0696
Chorismate mutase/prephenate dehydrogenase; Similar to SP:Q02287 GB:M74135 GB:X60420 PID:415010 PID:43345; identified by sequence similarity; putative.
    
 0.768
pyrI
Aspartate carbamoyltransferase, regulatory subunit; Involved in allosteric regulation of aspartate carbamoyltransferase.
  
    0.707
pyrB
Aspartate carbamoyltransferase, catalytic subunit; Similar to PID:1708787; identified by sequence similarity; putative.
  
    0.697
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
 
 
 0.679
VC_0355
Conserved hypothetical protein; Identified by Glimmer2; putative.
 
  
 0.625
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 
 0.610
fusA1
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
   
 0.596
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.