STRINGSTRING
RB2654_22348 protein (Maritimibacter alkaliphilus) - STRING interaction network
"RB2654_22348" - Apolipoprotein N-acyltransferase in Maritimibacter alkaliphilus
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:
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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
RB2654_22348Apolipoprotein N-acyltransferase ; Transfers the fatty acyl group on membrane lipoproteins (523 aa)    
Predicted Functional Partners:
RB2654_22353
Signal peptidase II ; This protein specifically catalyzes the removal of signal peptides from prolipoproteins (157 aa)
 
   
  0.949
RB2654_22368
Peptidase M23B (372 aa)
 
        0.910
RB2654_22358
Uncharacterized protein (260 aa)
              0.863
RB2654_22343
Uncharacterized protein (55 aa)
              0.861
RB2654_22363
Uncharacterized protein (152 aa)
              0.784
argS
Arginyl-tRNA synthetase (572 aa)
         
  0.685
hslU
Unfoldase HslU ; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (435 aa)
         
  0.617
secD
Protein translocase subunit SecD ; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (555 aa)
 
   
  0.615
RB2654_22298
Prolipoprotein diacylglyceryl transferase ; Transfers the N-acyl diglyceride group on what will become the N-terminal cysteine of membrane lipoproteins (301 aa)
 
   
  0.614
secF
Protein-export membrane protein SecF ; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (322 aa)
 
   
  0.613
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
Server load: low (8%) [HD]