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
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Textmining
[Homology]
Score
ruvBHolliday junction DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. (301 aa)    
Predicted Functional Partners:
ruvA
Holliday junction ATP-dependent DNA helicase ruvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
 
 
 0.999
ruvC
Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
 
 
 0.946
EGZ49153.1
Flagellar rod assembly protein/muramidase FlgJ; TIGRFAM: Flagellar protein FlgJ type-2; PFAM: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase; Flagellar protein FlgJ, N-terminal; KEGG: tgr:Tgr7_1225 flagellar rod assembly protein/muramidase FlgJ; SMART: Lysozyme domain, subfamily 2.
   
   0.878
queA
S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
 
  
 0.826
fliE
TIGRFAM: Flagellar hook-basal body complex protein FliE; HAMAP: Flagellar hook-basal body complex protein FliE; KEGG: tgr:Tgr7_1970 flagellar hook-basal body protein FliE; PFAM: Flagellar hook-basal body complex protein FliE.
    
   0.808
EGZ49428.1
Signal transduction histidine kinase with CheB and CheR activity; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family.
   
 
 0.781
EGZ49620.1
MCP methyltransferase/methylesterase, CheR/CheB with PAS/PAC sensor; PFAM: MCP methyltransferase, CheR-type, SAM-binding domain, C-terminal; Signal transduction response regulator, chemotaxis, protein-glutamate methylesterase; MCP methyltransferase, CheR-type, all-alpha domain, N-terminal; PAS fold-4; KEGG: alv:Alvin_2882 MCP methyltransferase/methylesterase, CheR/CheB with PAS/PAC sensor; SMART: MCP methyltransferase, CheR-type; PAS.
   
   0.759
EGZ50629.1
MCP methyltransferase, CheR-type; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
    
   0.755
EGZ49869.1
PFAM: MCP methyltransferase, CheR-type, SAM-binding domain, C-terminal; KEGG: mag:amb3003 methylase of chemotaxis methyl-accepting protein; SMART: MCP methyltransferase, CheR-type.
    
   0.755
EGZ46921.1
PFAM: MCP methyltransferase, CheR-type, SAM-binding domain, C-terminal; MCP methyltransferase, CheR-type, all-alpha domain, N-terminal; KEGG: psb:Psyr_0783 protein-glutamate O-methyltransferase; SMART: MCP methyltransferase, CheR-type.
    
   0.755
Your Current Organism:
Thiorhodospira sibirica
NCBI taxonomy Id: 765914
Other names: T. sibirica ATCC 700588, Thiorhodospira sibirica A12, Thiorhodospira sibirica ATCC 700588, Thiorhodospira sibirica str. ATCC 700588, Thiorhodospira sibirica strain ATCC 700588
Server load: low (12%) [HD]
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