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:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AGB33103.1Membrane protease subunit, stomatin/prohibitin; PFAM: SPFH domain / Band 7 family. (394 aa)    
Predicted Functional Partners:
AGB33104.1
Membrane protein implicated in regulation of membrane protease activity; PFAM: NfeD-like.
  
 
 0.841
AGB30602.1
NADH:ubiquinone oxidoreductase 49 kD subunit 7; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit.
   
 
 0.740
AGB32851.1
NADH:ubiquinone oxidoreductase 49 kD subunit 7; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit.
   
 
 0.740
AGB33639.1
PFAM: GTPase of unknown function; TIGRFAM: small GTP-binding protein domain; IMG reference gene:2509882500_SP.
   
 0.672
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.
   
  
 0.665
AGB33106.1
PFAM: Pyruvate kinase, barrel domain; PEP-utilising enzyme, mobile domain; Pyruvate kinase, alpha/beta domain; TIGRFAM: pyruvate kinase; Belongs to the pyruvate kinase family.
  
 
 0.651
AGB33102.1
Hypothetical protein.
       0.628
dnaK
Chaperone protein DnaK; Acts as a chaperone.
  
 0.617
pan
26S proteasome subunit P45 family; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-2 [...]
   
 
 0.580
pan-2
26S proteasome subunit P45 family; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-2 [...]
   
 
 0.580
Your Current Organism:
Natrinema pellirubrum
NCBI taxonomy Id: 797303
Other names: N. pellirubrum DSM 15624, Natrinema pellirubrum DSM 15624, Natrinema pellirubrum JCM 10476, Natrinema pellirubrum NCIMB 786, Natrinema pellirubrum str. DSM 15624, Natrinema pellirubrum strain DSM 15624
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.