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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
KML43673.1Rod-share determining protein MreBH; Derived by automated computational analysis using gene prediction method: Protein Homology. (335 aa)    
Predicted Functional Partners:
KML38420.1
Rod shape-determining protein MreC; Involved in formation and maintenance of cell shape.
 
 
 0.984
KML43693.1
XRE family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.881
KML45291.1
Cell cycle protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family.
 
 
 
 0.742
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.
  
 
 0.737
KML44184.1
Cell cycle protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family.
 
 
 
 0.731
KML38419.1
Rod shape-determining protein MreD; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.696
tuf
Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
    
 
 0.692
ftsZ-2
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.
  
 
 0.663
secF
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; Belongs to the SecD/SecF family. SecD subfamily.
  
    0.641
miaA
tRNA delta(2)-isopentenylpyrophosphate transferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family.
  
    0.637
Your Current Organism:
Bacillus firmus
NCBI taxonomy Id: 1399
Other names: ATCC 14575, B. firmus, BCRC 11730, Bacillaceae bacterium HQ2, Bacillus sp. JP44SK20, Bacillus sp. LK28, Bacillus sp. NCIM 2264, Bacillus sp. NCIM 2462, CCM 2213, CCRC 11730, CCRC:11730, CCUG 7418, CIP 52.70, DSM 12, IAM 12464, IFO 15306, JCM 2512, LMG 7125, LMG:7125, NBRC 15306, NCAIM B.01087, NCCB 48015, NCIB 9366, NCIMB 9366, NCTC 10335, NRRL B-14307, NRRL NRS-613, VKM B-498
Server load: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.