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
AFZ73140.1ATPase involved in chromosome partitioning; PFAM: CobQ/CobB/MinD/ParA nucleotide binding domain. (262 aa)    
Predicted Functional Partners:
AFZ71703.1
Putative transcriptional regulator containing CBS domains; PFAM: CBS domain; ParB-like nuclease domain.
  
 
 0.851
AFZ73141.1
Chemotaxis signal transduction protein; PFAM: CheW-like domain.
  
 
 0.823
ligA
DNA ligase, NAD-dependent; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
 
    0.609
srp54
Signal recognition particle GTPase; 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. Belongs to the GTP-binding SRP family. SRP54 subfamily.
  
    0.569
AFZ73277.1
PFAM: Protein phosphatase 2C; FHA domain.
 
  
 0.543
AFZ73139.1
Hypothetical protein.
       0.538
hisS
PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
    0.521
ftsZ-2
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.
 
  
 0.513
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.
 
  
 0.510
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
  
    0.493
Your Current Organism:
Natronobacterium gregoryi
NCBI taxonomy Id: 797304
Other names: N. gregoryi SP2, Natronobacterium gregoryi ATCC 43098, Natronobacterium gregoryi JCM 8860, Natronobacterium gregoryi NCIMB 2189, Natronobacterium gregoryi SP2, Natronobacterium gregoryi str. SP2, Natronobacterium gregoryi strain SP2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.