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
A6P07_01100Hypothetical protein. (79 aa)    
Predicted Functional Partners:
mrdA_1
Peptidoglycan D,D-transpeptidase MrdA.
       0.575
rplY
50S ribosomal protein L25; This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
       0.557
pth
Peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
       0.555
ychF
Ribosome-binding ATPase YchF; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner.
       0.549
Your Current Organism:
Acidithiobacillus thiooxidans
NCBI taxonomy Id: 930
Other names: A. thiooxidans, ATCC 19377, CIP 104597, DSM 14887, JCM 3867, NCIMB 8343, Thiobacillus concretivorus, Thiobacillus crenatus, Thiobacillus lobatus, Thiobacillus thermitanus, Thiobacillus thiooxidans, Thiobacillus umbonatus, Thiobacterium thiooxydans
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