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.
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:
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Cooccurrence
Coexpression
Experiments
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[Homology]
Score
minCSeptum 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; Belongs to the MinC family. (221 aa)    
Predicted Functional Partners:
Swoo_2113
TIGRFAM: septum site-determining protein MinD; PFAM: Cobyrinic acid ac-diamide synthase; KEGG: sse:Ssed_2520 septum site-determining protein MinD.
 
 
 0.998
Swoo_4628
Hypothetical protein; KEGG: tko:TK0952 ATPase involved in chromosome partitioning, ParA/MinD family.
 
 
 0.987
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.
 
  
 0.957
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.
   
 
 0.944
Swoo_4401
Rod shape-determining protein MreC; Involved in formation and maintenance of cell shape.
  
  
 0.872
Swoo_4400
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.
  
  
 0.867
Swoo_2115
PFAM: protein of unknown function DUF709; KEGG: sse:Ssed_2518 protein of unknown function DUF709.
  
  
 0.689
ftsA
Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family.
   
  
 0.654
Swoo_4402
TIGRFAM: cell shape determining protein, MreB/Mrl family; PFAM: cell shape determining protein MreB/Mrl; KEGG: sse:Ssed_0558 cell shape determining protein, MreB/Mrl family.
  
  
 0.631
ffh
Signal recognition particle protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual componen [...]
  
  
 0.588
Your Current Organism:
Shewanella woodyi
NCBI taxonomy Id: 392500
Other names: S. woodyi ATCC 51908, Shewanella woodyi ATCC 51908, Shewanella woodyi str. ATCC 51908, Shewanella woodyi strain ATCC 51908
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.