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
GAB95415.1Hypothetical protein. (337 aa)    
Predicted Functional Partners:
secY
Preprotein translocase SecY subunit; 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.
  
 0.990
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.
  
  
 0.983
secD
Protein-export membrane protein 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.
   
 0.982
GAB95414.1
Hypothetical protein; Could be involved in insertion of integral membrane proteins into the membrane; Belongs to the UPF0161 family.
  
  
 0.981
GAB95416.1
Hypothetical protein.
 
  
 0.980
secG
Protein-export membrane protein SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
   
 0.976
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.
  
 0.972
secE
Preprotein translocase SecE subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
  
 0.968
rpmH
50S ribosomal protein L34; Belongs to the bacterial ribosomal protein bL34 family.
  
  
 0.946
atpE
ATP synthase subunit c; 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.
 
 
 0.929
Your Current Organism:
Kineosphaera limosa
NCBI taxonomy Id: 1184609
Other names: K. limosa NBRC 100340, Kineosphaera limosa Lpha5, Kineosphaera limosa NBRC 100340, Kineosphaera limosa str. NBRC 100340, Kineosphaera limosa strain NBRC 100340, [uncultured] High G+C Gram-positive bacterium Lpha5
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.