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gid protein (Staphylococcus xylosus) - STRING interaction network
"gid" - Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO in Staphylococcus xylosus
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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gidMethylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO; Catalyzes the folate-dependent formation of 5-methyl- uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily (435 aa)    
Predicted Functional Partners:
topA
DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA super [...] (688 aa)
   
        0.739
xerC
annotation not available (296 aa)
              0.715
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (180 aa)
              0.715
hslU
ATP-dependent protease ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (469 aa)
              0.601
codY
GTP-sensing transcriptional pleiotropic repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor (257 aa)
              0.587
AID42946.1
annotation not available (586 aa)
         
  0.581
AID42988.1
annotation not available (292 aa)
              0.570
sucD
Succinate--CoA ligase [ADP-forming] subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit (301 aa)
              0.500
sucC
Succinate--CoA ligase [ADP-forming] subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (388 aa)
              0.496
AID42992.1
Ribosome biogenesis GTPase A; Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity (286 aa)
   
        0.490
Your Current Organism:
Staphylococcus xylosus
NCBI taxonomy Id: 1288
Other names: ATCC 29971, CCUG 7324, CIP 81.66, DSM 20266, HAMBI 2057, JCM 2418, NCTC 11043, NRRL B-14776, S. xylosus, Staphylococcus xylosus
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