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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
ORV07867.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (131 aa)    
Predicted Functional Partners:
sigA
RNA polymerase subunit sigma; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
     
 0.803
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.
 
 0.740
fusA
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.
   
  0.710
ORV10739.1
Elongation factor G; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.710
ORV09280.1
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
   
 0.660
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.
  
 
 0.637
ORV11337.1
2-keto-4-pentenoate hydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.635
ORV19702.1
Aldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aldehyde dehydrogenase family.
   
 0.546
ORV19619.1
Aldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aldehyde dehydrogenase family.
   
 0.546
gabD2
NADP-dependent semialdehyde dehydrogenase; part of alternative pathway from alpha-ketoglutarate to succinate; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.546
Your Current Organism:
Mycobacterium celatum
NCBI taxonomy Id: 28045
Other names: ATCC 51131, CCUG 39185, CDC 90-0899, CIP 106109, DSM 44243, JCM 12373, M. celatum, NCTC 13729
Server load: medium (54%) [HD]
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