STRINGSTRING
phoH2 phoH2 ybeY ybeY recO recO bex bex Cgl2286 Cgl2286 Cgl2289 Cgl2289 dnaJ2 dnaJ2 uppS2 uppS2 hemN hemN hrcA hrcA rsfS rsfS
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
phoH2Phosphate starvation-inducible protein. (339 aa)    
Predicted Functional Partners:
ybeY
Predicted metal-dependent hydrolase; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
 
  
 0.988
recO
Recombinational DNA repair protein (RecF pathway); Involved in DNA repair and RecF pathway recombination.
  
    0.931
bex
BEX PROTEIN (GTP-BINDING PROTEIN ERA HOMOLOG); An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
 
  
 0.918
Cgl2286
Putative membrane protein containing CBS domain.
  
    0.855
Cgl2289
Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
  
    0.726
dnaJ2
Molecular chaperone (contain C-terminal Zn finger domain), putative transcriptional repressor; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the react [...]
  
  
 0.724
uppS2
PUTATIVE UNDECAPRENYL DIPHOSPHATE SYNTHASE; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
  
    0.638
hemN
PUTATIVE ANAEROBIC COPROPORPHYRINOGEN III OXIDASE; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
     
 0.624
hrcA
Transcriptional regulator of heat shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
       0.621
rsfS
Conserved hypothetical protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
 
    0.602
Your Current Organism:
Corynebacterium glutamicum
NCBI taxonomy Id: 196627
Other names: C. glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum str. ATCC 13032, Corynebacterium glutamicum strain ATCC 13032
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.