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
EGZ48960.1KEGG: tgr:Tgr7_1721 radical SAM domain-containing protein. (445 aa)    
Predicted Functional Partners:
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.
   
   0.846
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.
    
   0.835
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.
    
   0.835
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.
    
   0.835
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.
    
   0.835
EGZ45727.1
MCP methyltransferase, CheR-type; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
    
   0.835
EGZ45426.1
PFAM: MCP methyltransferase, CheR-type, SAM-binding domain, C-terminal; MCP methyltransferase, CheR-type, all-alpha domain, N-terminal; KEGG: tgr:Tgr7_1216 MCP methyltransferase, CheR-type; SMART: MCP methyltransferase, CheR-type.
    
   0.835
EGZ44815.1
Pyruvate dehydrogenase (NADP(+))., Pyruvate synthase; KEGG: hha:Hhal_0066 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; 4Fe-4S binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
   
 
 0.799
bioB
Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.
    
 0.552
EGZ46257.1
Acetylornithine deacetylase; PFAM: Peptidase M20; Peptidase M20, dimerisation; TIGRFAM: Acetylornithine deacetylase (ArgE); HAMAP: Acetylornithine deacetylase; KEGG: tgr:Tgr7_0573 acetylornithine deacetylase.
  
 
 0.530
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
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