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
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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. (233 aa)    
Predicted Functional Partners:
Ping_1078
TIGRFAM: septum site-determining protein MinD; PFAM: Cobyrinic acid a,c-diamide synthase; KEGG: pha:PSHAb0506 cell division inhibitor, membrane ATPase, activates MinC.
 
 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.
 
  
 0.964
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
Ping_1124
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
Ping_1123
Rod shape-determining protein MreC; Involved in formation and maintenance of cell shape.
  
  
 0.834
Ping_1076
PFAM: protein of unknown function DUF709; KEGG: sdn:Sden_1630 protein of unknown function DUF709.
  
  
 0.670
Ping_1075
TIGRFAM: lytic murein transglycosylase; KEGG: ilo:IL1824 membrane-bound lytic murein transglycosylase.
  
    0.629
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.
   
  
 0.619
ffh
Signal recognition particle subunit FFH/SRP54 (srp54); 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 i [...]
  
  
 0.616
Ping_1122
TIGRFAM: cell shape determining protein, MreB/Mrl family; PFAM: cell shape determining protein MreB/Mrl; KEGG: ppr:PBPRA3270 putative MreB, Actin-like ATPase involved in cell morphogenesis.
  
  
 0.603
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.