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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Co-expression
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[Homology]
Score
ANS65653.1Signal peptidase; Belongs to the peptidase S26 family. (175 aa)    
Predicted Functional Partners:
secD-2
Bifunctional preprotein translocase subunit SecD/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; Belongs to the SecD/SecF family. SecD subfamily.
  
  
 0.760
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.
  
  
 0.735
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.
   
 
 0.733
tatB
Sec-independent translocase; 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.
  
  
 0.696
tatC
Integral membrane protein; 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.
  
  
 0.655
lepA
GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
  
 
 0.598
ANS69345.1
Non-hemolytic phospholipase C.
      
 0.598
ANS70102.1
Non-hemolytic phospholipase C.
      
 0.598
rnhB
Ribonuclease HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
  
  
 0.590
ANS65652.1
Putative PTS mannose-specific enzyme IIBCA component.
  
    0.549
Your Current Organism:
Streptomyces lincolnensis
NCBI taxonomy Id: 1915
Other names: ATCC 25466, BCRC 11173, CBS 630.70, CBS 699.69, CCRC 11173, CCRC:11173, DSM 2013, DSM 40355, IFO 13054, ISP 5355, JCM 4287, JCM 4488, KCTC 9088, KCTC 9089, NBRC 13054, NCIMB 9413, NRRL 2936, NRRL-ISP 5355, S. lincolnensis, VKM Ac-727
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