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
DvMF_2356Transcriptional regulator, XRE family; PFAM: helix-turn-helix domain protein; Cupin 2 conserved barrel domain protein; KEGG: dde:Dde_0556 MerR family transcriptional regulator. (188 aa)    
Predicted Functional Partners:
DvMF_2357
PFAM: AMP-dependent synthetase and ligase; KEGG: dde:Dde_0557 acyl-CoA synthetase.
 
   
 0.883
DvMF_0409
TIGRFAM: CDP-diacylglycerol/glycerol-3-phosphate 3-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; KEGG: dde:Dde_2074 CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
 
    0.782
DvMF_0344
TIGRFAM: cell shape determining protein, MreB/Mrl family; PFAM: cell shape determining protein MreB/Mrl; KEGG: dde:Dde_1993 rod shape-determining protein MreB.
  
 
 0.737
DvMF_2820
TIGRFAM: cell shape determining protein, MreB/Mrl family; PFAM: cell division protein FtsA; cell shape determining protein MreB/Mrl; KEGG: dde:Dde_0996 rod shape-determining protein MreB.
  
 
 0.737
secA
Preprotein translocase, SecA subunit; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.
  
 
 0.680
rplF
Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
   
   0.669
rplM
Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
   0.658
rplW
Ribosomal protein L25/L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family.
    
 
 0.648
rplS
Ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
  
   0.647
rplV
Ribosomal protein L22; This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).
    
   0.645
Your Current Organism:
Desulfovibrio vulgaris Miyazaki
NCBI taxonomy Id: 883
Other names: D. vulgaris str. 'Miyazaki F', Desulfovibrio vulgaris (strain Miyazaki), Desulfovibrio vulgaris str. 'Miyazaki F'
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.