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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
VC_A0990ATP-dependent RNA helicase, DEAD box family; Similar to GB:L02123 SP:P25888 PID:560801 GB:U00096 PID:1651360; identified by sequence similarity; putative; Belongs to the DEAD box helicase family. (428 aa)    
Predicted Functional Partners:
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
  
 
 0.800
rplC
Ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
   
 
 0.786
rplD
Ribosomal protein L4; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). As the V.cholerae S10 leader can be regulated in vitro by the E.coli L4 protein this suggests the endogenous protein controls its own S10 operon in a similar fashion.
   
 0.784
nnr
Conserved hypothetical protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity). In the N-terminal section; belongs to the NnrE/AIBP family.
   
 0.754
VC_A0528
Conserved hypothetical protein; Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity; Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.
  
 0.736
rplM
Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
   
 0.722
rplJ
Ribosomal protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family.
   
 
 0.717
rplK
Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
 
 0.711
rlmE
Cell division protein FtsJ; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
   
 0.703
VC_1636
Helicase-related protein; Similar to SP:P36927 GB:U00096; identified by sequence similarity; putative.
   
 0.702
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
Server load: medium (58%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.