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gidA protein (Xanthomonas campestris campestris) - STRING interaction network
"gidA" - tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG in Xanthomonas campestris campestris
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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gidAtRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34; Belongs to the MnmG family (634 aa)    
Predicted Functional Partners:
mnmE
tRNA modification GTPase MnmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- like GTPase superfamily. TrmE GTPase family (446 aa)
 
  0.996
rsmG
Ribosomal RNA small subunit methyltransferase G; Specifically methylates the N7 position of guanine in position 527 of 16S rRNA (314 aa)
   
  0.990
mnmA
tRNA-specific 2-thiouridylase MnmA; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34 (378 aa)
 
 
  0.865
yidC
Membrane protein insertase YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (575 aa)
   
   
  0.793
dnaA
Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box)- 5’-TTATC[CA]A[CA]A-3’. DnaA binds to ATP and to acidic phospholipids (442 aa)
   
   
  0.787
lepA
Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner (601 aa)
 
   
  0.785
prfA
Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA (361 aa)
 
   
  0.783
rnpA
Ribonuclease P protein component; RNaseP catalyzes the removal of the 5’-leader sequence from pre-tRNA to produce the mature 5’-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5’-leader sequence and broadening the substrate specificity of the ribozyme (148 aa)
   
   
  0.743
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (927 aa)
   
   
  0.736
prfB
Peptide chain release factor 2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (313 aa)
 
 
  0.727
Your Current Organism:
Xanthomonas campestris campestris
NCBI taxonomy Id: 340
Other names: X. campestris pv. campestris, Xanthomonas campestris, Xanthomonas campestris (pv. campestris), Xanthomonas campestris campestris, Xanthomonas campestris pv. campestris
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