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
YPO0934Conserved 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. (243 aa)    
Predicted Functional Partners:
prmA
Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.
 
  
 0.890
gsh-II
Similar to Escherichia coli glutathione synthetase GshB SW:GSHB_ECOLI (P04425) (316 aa) fasta scores: E(): 0,80.1% id in 317 aa, and to Vibrio cholerae glutathione synthetase VC0468 TR:Q9KUP7 (EMBL:AE004133) (318 aa) fasta scores: E(): 0, 73.9% id in 314 aa.
  
  
 0.787
dnaJ
Chaperone protein DnaJ; 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 reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
  
   0.673
yqgF
Conserved hypothetical protein; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF nuclease family.
  
  
 0.626
YPO0936
Conserved hypothetical protein; Similar to Escherichia coli protein YqgE SW:YQGE_ECOLI (P52049) (187 aa) fasta scores: E(): 0, 66.8% id in 187 aa, and to Vibrio cholerae hypothetical protein VC0467 TR:Q9KUP8 (EMBL:AE004133) (200 aa) fasta scores: E(): 0, 51.6% id in 190 aa; Belongs to the UPF0301 (AlgH) family.
  
  
 0.609
gidB
Glucose inhibited division protein B; Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
 
  
 0.572
sprT
Similar to Escherichia coli hypothetical protein SprT SW:SPRT_ECOLI (P39902) (165 aa) fasta scores: E(): 0,69.8% id in 162 aa, and to Haemophilus influenzae hypothetical protein HI1173 SW:SPRT_HAEIN (P44119) (156 aa) fasta scores: E(): 1.8e-30, 52.0% id in 148 aa.
  
  
 0.530
endA
Similar to Escherichia coli endonuclease I EndA SW:END1_ECOLI (P25736) (235 aa) fasta scores: E(): 0, 74.0% id in 235 aa, and to Erwinia chrysanthemi nuclease NucM SW:NUCM_ERWCH (P37994) (266 aa) fasta scores: E(): 0, 75.7% id in 230 aa. Orthologues are periplasmic proteins. CDS is predicted to have an uncleavable N-terminal signal sequence. Effect on the function is unknown.
  
    0.511
trmD
tRNA (guanine-N1)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family.
 
  
 0.511
miaB
Putative tRNA-thiotransferase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
  
  
 0.504
Your Current Organism:
Yersinia pestis
NCBI taxonomy Id: 214092
Other names: Y. pestis CO92, Yersinia pestis CO92, Yersinia pestis str. CO92, Yersinia pestis strain CO92
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