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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
ugtPDiacylglycerol glucosyltransferase; Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta- monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D- glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O- (beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D- glucopyranosyl)-1,2-diacyl- [...] (381 aa)    
Predicted Functional Partners:
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.
  
 
 0.870
murD
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family.
  
 
 0.842
murF
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D- alanine ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily.
  
 
 0.829
murC
UDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
  
 
 0.791
murE
UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily.
 
 0.724
ftsH
Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
   
  
 0.664
KEZ52954.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.653
murE-2
UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
  
 0.651
KEZ51748.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.636
ddl
D-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
  
  
 0.606
Your Current Organism:
Bacillus indicus
NCBI taxonomy Id: 246786
Other names: B. indicus, Bacillus cibi, Bacillus cibi Yoon et al. 2005, Bacillus indicus Suresh et al. 2004 emend. Stropko et al. 2014, Bacillus sp. KU12, Bacillus sp. KU14, DSM 15820, DSM 16189 [[Bacillus cibi]], JCM 12168, KCTC 3880 [[Bacillus cibi]], LMG 22858, LMG:22858, MTCC 4374, strain JG-30 [[Bacillus cibi]], strain Sd/3
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