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Mettu_2904 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2904" - Putative signal transduction protein in Methylobacter tundripaludum
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.
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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:
some 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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Gene Fusion
Cooccurence
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[Homology]
Score
Mettu_2904Putative signal transduction protein; PFAM- Metal-dependent hydrolase HDOD; KEGG- nwa-Nwat_0678 putative signal transduction protein (280 aa)    
Predicted Functional Partners:
Mettu_2903
PFAM- Cytochrome oxidase assembly; KEGG- mca-MCA1778 cytochrome oxidase assembly protein (322 aa)
              0.823
Mettu_2905
Folate-binding protein YgfZ; KEGG- tgr-Tgr7_1464 glycine cleavage T protein (aminomethyl transferase); TIGRFAM- Folate-binding, YgfZ; PFAM- Glycine cleavage T-protein, N-terminal; Belongs to the GcvT family (326 aa)
              0.745
Mettu_3665
Cyclic diguanosine monophosphate-binding protein; Binds the second messenger bis-(3’-5’) cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second- messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein (122 aa)
   
          0.720
Mettu_0096
Flagellar protein FliL; Controls the rotational direction of flagella during chemotaxis (167 aa)
   
          0.714
Mettu_3577
Flagellar protein FliL; Controls the rotational direction of flagella during chemotaxis (154 aa)
   
          0.675
Mettu_4075
PFAM- Type IV pilus assembly PilZ; KEGG- dak-DaAHT2_1202 type IV pilus assembly PilZ (202 aa)
   
          0.672
Mettu_2597
KEGG- alv-Alvin_2068 putative signal transduction protein; PFAM- Metal-dependent hydrolase HDOD; SMART- GAF (513 aa)
   
          0.659
Mettu_2434
KEGG- gpb-HDN1F_00940 adenylate cyclase; PFAM- Adenylate cyclase, class-I (934 aa)
   
          0.601
Mettu_3269
KEGG- nhl-Nhal_3565 adenylate cyclase; PFAM- Adenylate cyclase, class-I (936 aa)
   
          0.600
Mettu_1247
Flagella basal body P-ring formation protein FlgA; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P-ring assembly (232 aa)
 
          0.599
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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