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
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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.
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experimentally determined
co-expression
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gene neighborhood
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[Homology]
Score
KRV51006.1Signal peptidase I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family. (274 aa)    
Predicted Functional Partners:
KRV51181.1
Signal peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family.
 
  
 
0.959
KRV51182.1
Signal peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family.
 
  
 
0.929
KRV51005.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family.
 
    
0.727
rimM
16S rRNA processing protein RimM; An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes; Belongs to the RimM family.
 
    0.722
rplS
50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
  
  
 0.691
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.
  
 
 0.686
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
 
   
 0.674
KRV51010.1
DNA polymerase III subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.669
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.
 
  
 0.655
KRV47317.1
Preprotein translocase YidC; Functions to insert inner membrane proteins into the IM in Escherichia coli; interacts with transmembrane segments; functions in both Sec-dependent and -independent membrane insertion; similar to Oxa1p in mitochondria; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.646
Your Current Organism:
Streptomyces vitaminophilus
NCBI taxonomy Id: 76728
Other names: ATCC 31673, Actinosporangium vitaminiphilum, Actinosporangium vitaminophilum, DSM 41686, IFO 14294, JCM 6054, NBRC 14294, NRRL B-16933, S. vitaminophilus, Streptomyces vitaminiphilus, Streptomyces vitaminophileus, strain SF 2080
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