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JG24_15655 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_15655" - Septum site-determining protein MinD in Klebsiella pneumoniae
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
JG24_15655Septum site-determining protein MinD; ATPase; with MinC inhibits cell division by blocking formation of the polar Z ring septums; Derived by automated computational analysis using gene prediction method- Protein Homology (270 aa)    
Predicted Functional Partners:
minE
Cell division topological specificity factor; Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell (89 aa)
 
  0.999
minC
Probable septum site-determining protein MinC; Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization (233 aa)
 
  0.999
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 (383 aa)
   
 
  0.670
JG24_15640
YcgL domain-containing protein; Derived by automated computational analysis using gene prediction method- Protein Homology (93 aa)
              0.645
rne
Bifunctional ribonuclease E/endoribonuclease/RNA-binding protein/RNA degradosome binding protein; forms part of the membrane-associated degradosome complex along with PNPase, RhlB, and enolase; Derived by automated computational analysis using gene prediction method- Protein Homology (1082 aa)
     
      0.592
JG24_15635
FIG094199- Fumarylacetoacetate hydrolase; Derived by automated computational analysis using gene prediction method- Protein Homology (219 aa)
              0.554
JG24_23170
Cytoplasmic axial filament protein CafA and Ribonuclease G; Involved in the processing of the 5’end of 16S rRNA; Derived by automated computational analysis using gene prediction method- Protein Homology (489 aa)
     
      0.524
rlmB
23S rRNA (guanosine-2’-O-)-methyltransferase RlmB; Specifically methylates the ribose of guanosine 2251 in 23S rRNA; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. RlmB subfamily (243 aa)
           
  0.521
rpsN
30S ribosomal protein S14; Located in the peptidyl transferase center and involved in assembly of 30S ribosome subunit; similar to what is observed with proteins L31 and L33, some proteins in this family contain CXXC motifs that are involved in zinc binding; if two copies are present in a genome, then the duplicated copy appears to have lost the zinc-binding motif and is instead regulated by zinc; the proteins in this group do not appear to have the zinc-binding motif; Derived by automated computational analysis using gene prediction method- Protein Homology (101 aa)
         
  0.497
rpmD
50S ribosomal protein L30; L30 binds domain II of the 23S rRNA and the 5S rRNA; similar to eukaryotic protein L7; Derived by automated computational analysis using gene prediction method- Protein Homology (59 aa)
           
  0.491
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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