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
yidCHypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (439 aa)    
Predicted Functional Partners:
secD
Preprotein 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.
   
 0.949
secF
Preprotein translocase subunit 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.
   
 0.903
atpE
ATP synthase F0F1 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.
  
 
 0.899
rpsI
30S ribosomal protein S9; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS9 family.
   
   0.798
rplQ
50S ribosomal protein L17; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.794
secY
Preprotein 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.
   
 0.764
KGL12681.1
Preprotein translocase subunit SecY; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.764
rho
Transcription termination factor Rho; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.
  
  
 0.754
KGL13702.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.752
metG
methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
  
 0.709
Your Current Organism:
Helicobacter muridarum
NCBI taxonomy Id: 216
Other names: ATCC 49282, CCUG 29262, CIP 104248, DSM 22221, H. muridarum, LMG 13646, LMG:13646, NCTC 12714, strain ST1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.