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RB2654_05145 protein (Maritimibacter alkaliphilus) - STRING interaction network
"RB2654_05145" - Membrane protein, putative in Maritimibacter alkaliphilus
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query proteins and first shell of interactors
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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_05145Membrane protein, putative (290 aa)    
Predicted Functional Partners:
RB2654_05140
Membrane protein, putative (290 aa)
 
       
0.711
RB2654_20033
ABC transporter, ATP binding/permease protein (593 aa)
   
      0.706
RB2654_17906
ABC multidrug efflux pump, fused ATPase and inner membrane subunits (610 aa)
   
      0.706
RB2654_17901
ABC multidrug efflux pump, fused ATPase and inner membrane subunits (607 aa)
   
      0.706
RB2654_12234
ATP-binding protein of ABC transporter (617 aa)
   
      0.706
RB2654_04154
Phosphatidate cytidylyltransferase (286 aa)
     
      0.527
truA
tRNA-uridine isomerase I ; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs (257 aa)
   
        0.485
RB2654_05135
Possible flagellar motor switch protein (FliG) (345 aa)
              0.477
tgt
tRNA-guanine transglycosylase ; Exchanges the guanine residue with 7-aminomethyl-7- deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (380 aa)
   
        0.445
secY
Protein translocase subunit SecY ; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (451 aa)
     
      0.442
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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