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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
ndhNADH dehydrogenase; Identified by similarity to SP:P00393; match to protein family HMM PF00070; match to protein family HMM PF07992. (440 aa)    
Predicted Functional Partners:
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
 
 
   0.759
MCA1919
Hypothetical protein; Identified by Glimmer2; putative.
       0.645
atpD-1
ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.
   
  
 0.629
nuoCD
NADH dehydrogenase I, C/D subunits; 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.
     
 0.513
MCA0162
Hydrogenase expression/formation protein; Identified by similarity to SP:Q03004; match to protein family HMM PF01750; match to protein family HMM TIGR00072; match to protein family HMM TIGR00140; match to protein family HMM TIGR00141.
    
 
 0.469
MCA0879
Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
     
 0.445
relA
GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
       0.433
MCA0769
Pyruvate ferredoxin/flavodoxin oxidoreductase family protein; Identified by similarity to SP:P52647; match to protein family HMM PF00037; match to protein family HMM PF01558; match to protein family HMM PF01855; match to protein family HMM PF02775; match to protein family HMM TIGR02176.
   
  
 0.432
MCA3004
Pyridine nucleotide-disulphide oxidoreductase family protein; Identified by match to protein family HMM PF00070; match to protein family HMM PF00581; match to protein family HMM PF02852; match to protein family HMM PF07992.
 
  
 0.424
atpE-1
ATP synthase F0, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
   
  
 0.420
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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