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
tatCSec-independent protein translocase TatC; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. (258 aa)    
Predicted Functional Partners:
tatB
Sec-independent protein translocase TatB; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
 
 0.998
tatA
Twin-arginine translocation protein, TatA/E family subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
 
 0.994
Ping_0317
Sec-independent protein translocase TatD; PFAM: TatD-related deoxyribonuclease; KEGG: cps:CPS_0167 deoxyribonuclease TatD.
     
 0.833
Ping_0316
Porphobilinogen synthase; PFAM: delta-aminolevulinic acid dehydratase; KEGG: vch:VC0105 delta-aminolevulinic acid dehydratase; Belongs to the ALAD family.
 
     0.812
Ping_0322
PFAM: protein of unknown function DUF1243; KEGG: vpa:VP0096 conserved hypothetical protein.
  
    0.615
ubiB
2-octaprenylphenol hydroxylase; Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
  
  
 0.607
ubiE
Demethylmenaquinone methyltransferase; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- methyl-6-methoxy-1,4-benzoquinol (DMQH2).
 
     0.545
Ping_2873
Fused ubiquinol-cytochrome c reductase and cytochrome b/b6; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
  
 0.478
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.
 
   
 0.459
secF
Protein 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.
 
   
 0.451
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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