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
KKF34509.1Protein CapI; Derived by automated computational analysis using gene prediction method: Protein Homology. (335 aa)    
Predicted Functional Partners:
KKF34508.1
UDP-glucose 6-dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.996
KKF34507.1
Together with GalF subunit composes the UTP--glucose-1-phosphate uridylyltransferase, an enzyme that catalyzes the formation of UDP-glucose from UTP and alpha-D-glucose 1-phosphate; regulates cellular levels of UDP-glucose; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.982
KKF35113.1
UTP--glucose-1-phosphate uridylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.951
arnA
UDP-4-amino-4-deoxy-L-arabinose formyltransferase; Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides; In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily.
    
 
0.941
rpsS
30S ribosomal protein S19; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
   
  0.934
rpsN
30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
   
  0.934
rpsL
30S ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
   
 0.933
rpsC
30S ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
   
  0.931
rpsQ
30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
   
  0.931
rpsH
30S ribosomal protein S8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
   
  0.927
Your Current Organism:
Erwinia tracheiphila
NCBI taxonomy Id: 65700
Other names: ATCC 33245, Bacillus tracheiphilus, Bacterium tracheiphilus, CFBP 2355, CIP 105205, DSM 21139, E. tracheiphila, Erwinia amylovora var. tracheiphila, ICMP 5845, LMG 2707, LMG 2906, LMG:2707, LMG:2906, NCPPB 2452
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