STRINGSTRING
sepF sepF ABS22781.1 ABS22781.1 ABS22783.1 ABS22783.1 ABS22780.1 ABS22780.1 ftsZ ftsZ ABS22779.1 ABS22779.1 ABS22784.1 ABS22784.1 ftsA ftsA ABS23324.1 ABS23324.1 ABS22621.1 ABS22621.1 gpsB gpsB
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
sepFProtein of unknown function DUF552; Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. (156 aa)    
Predicted Functional Partners:
ABS22781.1
PFAM: protein of unknown function YGGT; KEGG: bat:BAS3749 YlmG protein.
  
  
 0.959
ABS22783.1
Alanine racemase domain protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
  
  
 0.952
ABS22780.1
PFAM: RNA-binding S4 domain protein; KEGG: bce:BC3897 RNA binding protein.
 
  
 0.937
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.
  
 
 0.927
ABS22779.1
PFAM: DivIVA family protein; KEGG: btl:BALH_3527 cell-division initiation protein (divIVA).
  
  
 0.846
ABS22784.1
PFAM: protein of unknown function DUF152; KEGG: btl:BALH_3531 hypothetical protein; Belongs to the multicopper oxidase YfiH/RL5 family.
  
  
 0.809
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.
  
 
 0.777
ABS23324.1
PFAM: protein of unknown function DUF965; KEGG: bat:BAS4283 hypothetical protein; Belongs to the UPF0297 family.
  
    0.637
ABS22621.1
Aluminium resistance family protein; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; Aluminium resistance family protein; KEGG: bca:BCE_3733 hypothetical protein.
 
     0.625
gpsB
DivIVA family protein; Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation.
 
  
 0.623
Your Current Organism:
Bacillus cytotoxicus
NCBI taxonomy Id: 315749
Other names: B. cytotoxicus NVH 391-98, Bacillus cereus NVH 391-98, Bacillus cereus subsp. cytotoxicus NVH 391-98, Bacillus cereus subsp. cytotoxis NVH 391-98, Bacillus cytotoxicus NVH 391-98, Bacillus cytotoxicus str. NVH 391-98, Bacillus cytotoxicus strain NVH 391-98, Bacillus cytotoxis NVH 391-98
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.