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
proSProlyl tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). (480 aa)    
Predicted Functional Partners:
ileS
isoleucyl-tRNA synthase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
   
 0.966
metS
Putative methionyl-tRNA synthase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
  
 0.912
gltS
glutamyl-tRNA synthase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.902
argS
arginyl-tRNA synthase; Identical to the previously sequenced Mycobacterium leprae arginyl-tRNA synthetase (EC 6.1.1.19) (arginine--tRNA ligase) SW:SYR_MYCLE (P45840) (550 aa); Fasta score E(): 0, 99.6% identity in 550 aa overlap. Also highly similar to many other arginyl-tRNA synthetases including: Mycobacterium tuberculosis SW:SYR_MYCTU (Q10609) (550 aa); Fasta score E(): 0, 84.9% identity in 550 aa overlap and Brevibacterium lactofermentum SW:SYR_BRELA (P41253) (550 aa); Fasta score E(): 0, 63.8% identity in 550 aa overlap. Contains Pfam match to entry PF00750 tRNA-synt_1d, tRNA synt [...]
  
 0.897
leuS
leucyl-tRNA synthase; Similar to M. tuberculosis leuS, leucyl-tRNA synthetase, SW:SYL_MYCTU (P71698) (969 aa); Fasta score E(): 0, 83.6% identity in 972 aa overlap and to Bacillus subtilis leuS, leucyl-tRNA synthetase, SW:SYL_BACSU (P36430) (804 aa); Fasta score E(): 0, 45.7% identity in 941 aa overlap. Previously sequenced as SW:SYL_MYCLE (Q50192) (972 aa); Fasta score E(): 0, 99.9% identity in 972 aa overlap. Contains Pfam match to entry PF00133 tRNA-synt_1, tRNA synthetases class I (I, L, M and V). Contains PS00178 Aminoacyl-transfer RNA synthetases class-I signature.
  
 0.838
lysS
Putative lysyl-tRNA synthase; Similar to M. tuberculosis lysS, Rv3598c, putative lysyl-tRNA synthase, SW:SYK_MYCTU (O06284) (505 aa); Fasta score E(): 0, 85.4% identity in 501 aa overlap. Similar to Escherichia coli lysU, lysyl-tRNA synthase, SW:SYK2_ECOLI (P14825) (504 aa); Fasta score E(): 0, 38.8% identity in 497 aa overlap. Contains Pfam match to entry PF00152 tRNA-synt_2, tRNA synthetases class II (D, K and N). Contains PS00179 Aminoacyl-transfer RNA synthetases class-II signature 1; Similar to the C-terminal half of ML1393.
  
 0.781
pheT
phenylalanyl-tRNA synthase [beta] subunit; Highly similar to many phenylalanyl-tRNA synthetase beta chains including: Escherichia coli SW:SYFB_ECOLI (P07395) (795 aa); Fasta score E(): 0, 31.0% identity in 851 aa overlap and Mycobacterium tuberculosis RV1649 SW:SYFB_MYCTU (P94985) (831 aa); Fasta score E(): 0, 79.6% identity in 834 aa overlap.
  
 
 0.766
lysX
C-term lysyl-tRNA synthase; Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysin [...]
  
 0.765
thrS
threonyl-tRNA synthetase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
   
 
0.701
ML2186
Transcriptional regulator (NifR3/Smm1 family); Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family.
  
 
 0.676
Your Current Organism:
Mycobacterium leprae
NCBI taxonomy Id: 272631
Other names: M. leprae TN, Mycobacterium leprae TN, Mycobacterium leprae str. TN, Mycobacterium leprae strain TN
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