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
minDSeptum 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:
minC
Septum formation inhibitor; 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; Belongs to the MinC family.
 
 0.999
minE
Cell division topological specificity factor MinE; 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.
 
 0.999
mreC
Rod shape-determining protein MreC; In some organisms this protein is a transmembrane protein while in others it is periplasmic; involved in some organisms with other components of the MreBCD complex and with penicillin binding proteins in the periplasm or cell wall; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.749
lpxD
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase; Catalyzes the N-acylation of UDP-3-O- (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell; Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
 
      0.731
fabZ
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
 
      0.731
lpxA
acyl-[acyl-carrier-protein]--UDP-N- acetylglucosamine O-acyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
 
      0.731
AND15152.1
Rod shape-determining protein MreD; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins. Belongs to the MreD family.
  
  
 0.727
ycgL
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.561
AND13160.1
Lytic murein transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.527
mreB
Rod shape-determining protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.496
Your Current Organism:
Proteus mirabilis
NCBI taxonomy Id: 584
Other names: ATCC 29906, CCUG 26767, CIP 103181, DSM 4479, LMG 3257, LMG:3257, NCTC 11938, P. mirabilis
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.