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
rnrRibonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (743 aa)    
Predicted Functional Partners:
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
  
 0.995
smpB
SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...]
     
 0.773
secG
Preprotein translocase, SecG subunit; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
 
  
 0.658
hppA
V-type H(+)-translocating pyrophosphatase; Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane. Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-stimulated subfamily.
       0.597
rsmB
16S rRNA (cytosine(967)-C(5))-methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
 
 
 0.592
NPD11_135
RNA 2'-O ribose methyltransferase substrate binding family protein; [J] COG0566 rRNA methylases; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
  
 
 0.577
AQM60106.1
RNA 2'-O ribose methyltransferase substrate binding family protein; [J] COG0566 rRNA methylases; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
  
 
 0.577
eno
Phosphopyruvate hydratase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
 
 
 0.575
AQM60627.1
NUDIX domain protein; [LR] COG0494 NTP pyrophosphohydrolases including oxidative damage repair enzymes; Belongs to the Nudix hydrolase family.
   
 0.574
NPD11_352
NUDIX domain protein; [LR] COG0494 NTP pyrophosphohydrolases including oxidative damage repair enzymes.
   
 0.574
Your Current Organism:
Clostridium baratii
NCBI taxonomy Id: 1561
Other names: ATCC 27638, Acuformis perennis, BCRC 14541, C. baratii, CCRC 14541, CCRC:14541, CCUG 24033, CIP 104306, Clostridium barati, Clostridium paraperfringens, Clostridium perenne, DSM 601, Inflabilis barati
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