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
rlmLRibosomal RNA large subunit methyltransferase K/L; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Belongs to the methyltransferase superfamily. RlmKL family. (756 aa)    
Predicted Functional Partners:
ribD
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
     
 0.765
uup
ABC transporter ATP-binding protein uup.
  
 0.669
ispU
Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific); Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di- trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
  
    0.656
CEL27105.1
16S ribosomal RNA methyltransferase RsmE; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
 
  
 0.627
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction.
  
    0.624
rlmH
Ribosomal RNA large subunit methyltransferase H; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family.
 
  
 0.614
thiI
tRNA sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
  
  
 0.604
rlmB
23S rRNA (guanosine-2'-O-)-methyltransferase RlmB; Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
  
 
 0.598
argS
Arginine--tRNA ligase.
  
    0.573
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
     0.566
Your Current Organism:
Pseudomonas fluorescens
NCBI taxonomy Id: 294
Other names: ATCC 13525, Bacillus fluorescens, Bacillus fluorescens liquefaciens, Bacterium fluorescen, CCEB 546, CFBP 2102, CIP 69.13, DSM 50090, IAM 12022, IFO 14160, JCM 5963, Liquidomonas fluorescens, NBRC 14160, NCCB 76040, NCIB 9046, NCIB:9046, NCIMB 9046, NCTC 10038, NRRL B-14678, P. fluorescens, Pseudomonas sp. AU2390, Pseudomonas sp. BZ64, Pseudomonas sp. FY32, Pseudomonas sp. HSA2/2016, Pseudomonas sp. HSA3/2016, Pseudomonas sp. ISSDS-433, Pseudomonas sp. JCM 17186, Pseudomonas sp. JCM 2779, Pseudomonas sp. KH-20150KS3, Pseudomonas sp. LBUM223, Pseudomonas sp. LBUM636, Pseudomonas sp. SM2/2016, RH 818, VKM B-894, bacterium P1-1, strain M. Rhodes 28/5
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