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RB2654_15696 protein (Maritimibacter alkaliphilus) - STRING interaction network
"RB2654_15696" - SPFH domain/band 7 family protein in Maritimibacter alkaliphilus
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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[Homology]
Score
RB2654_15696SPFH domain/band 7 family protein (297 aa)    
Predicted Functional Partners:
RB2654_15701
Uncharacterized protein (91 aa)
              0.868
ftsH
ATP-dependent zinc metalloprotease FtsH ; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (630 aa)
 
 
  0.781
RB2654_11813
Uncharacterized protein (163 aa)
       
      0.743
RB2654_06514
Cytochrome c oxidase subunit 2 ; 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) (282 aa)
     
 
  0.722
RB2654_15691
NUDIX hydrolase (135 aa)
   
      0.657
RB2654_05732
Protein HflC ; HflC and HflK could regulate a protease (348 aa)
   
          0.628
hflX
GTP-binding protein HflX ; GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis (427 aa)
 
   
  0.600
RB2654_02329
Nicotinamide nucleotide repair protein ; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (546 aa)
   
        0.520
atpD
F-ATPase subunit beta ; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits (474 aa)
 
  0.507
purA
IMP--aspartate ligase ; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (431 aa)
   
        0.492
Your Current Organism:
Maritimibacter alkaliphilus
NCBI taxonomy Id: 314271
Other names: M. alkaliphilus, M. alkaliphilus HTCC2654, Maritimibacter, Maritimibacter Lee et al. 2007, Maritimibacter alkaliphilus, Maritimibacter alkaliphilus HTCC2654, Maritimibacter alkaliphilus Lee et al. 2007, Maritimibacter alkaliphilus str. HTCC2654, Maritimibacter alkaliphilus strain HTCC2654, Rhodobacterales bacterium HTCC2654
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