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
RPE_2196PFAM: protein-L-isoaspartate(D-aspartate) O-methyltransferase; Methyltransferase type 11; Methyltransferase type 12; KEGG: bja:bll7569 probable O-methyltransferase. (280 aa)    
Predicted Functional Partners:
RPE_2197
PFAM: short-chain dehydrogenase/reductase SDR; glucose/ribitol dehydrogenase; KEGG: rpc:RPC_3247 short-chain dehydrogenase/reductase SDR; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
  
    0.691
pcm
protein-L-isoaspartate O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
  
     0.649
RPE_2747
PFAM: protein-L-isoaspartate(D-aspartate) O-methyltransferase; Methyltransferase type 11; Methyltransferase type 12; KEGG: rpc:RPC_2567 protein-L-isoaspartate(D-aspartate) O-methyltransferase.
  
     0.612
ispE
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
   
    0.577
RPE_2198
PFAM: sulfatase; KEGG: rpc:RPC_3246 sulfatase.
 
     0.471
nuoC
NADH dehydrogenase I, D subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
  
   0.448
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
   
    0.445
surE
Exopolyphosphatase / 3'-nucleotidase / 5'-nucleotidase; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family.
  
  
 0.419
RPE_0966
Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
   
   0.417
RPE_1153
PFAM: flagellar motor switch protein FliG; KEGG: rpc:RPC_1092 flagellar motor switch protein FliG.
   
   0.417
Your Current Organism:
Rhodopseudomonas palustris BisA53
NCBI taxonomy Id: 316055
Other names: R. palustris BisA53, Rhodopseudomonas palustris str. BisA53, Rhodopseudomonas palustris strain BisA53
Server load: low (38%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.