Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Putative ribosome biogenesis GTPase RsgA |
Protein Synonyms/Alias | |
Gene Name | rsgA |
Gene Synonyms/Alias | engC, yloQ; OrderedLocusNames=BSU15780 |
Created Date | 3-June-2014 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Phosphorylation | Position | Peptide | Code | Type | References | 166 | IPHFQDKTTVFAGQS | T | LTP | [1] | |
Reference | [1]Phosphorylation of CpgA protein enhances both its GTPase activity and its affinity for ribosome and is crucial for Bacillus subtilis growth and morphology. Pompeo F,Freton C,Wicker-Planquart C,Grangeasse C,Jault JM,Galinier A J. Biol. Chem. 2012, Jun, 15;287(25):20830-8. [ PMID:22544754] |
Functional Description From UniProt | FUNCTION: Depletion of yloQ results in sensitization towards protein synthesis inhibitors that block the peptide channel or peptidyl transferase center on the ribosome, implying that YloQ functions in conjunction with the ribosome in vivo. Decreasing levels of YloQ lead to an increase in unassembled 30S and 50S subunit and a decrease in the assembled 70S ribosome |
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| 3D-structure; Completeproteome; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding; Referenceproteome; Zinc |
Protein Sequence | MPEGKIIKAL SGFYYVLDES EDSDKVIQCR GRGIFRKNKI TPLVGDYVVY QAENDKEGYL 60 MEIKERTNEL IRPPICNVDQ AVLVFSAVQP SFSTALLDRF LVLVEANDIQ PIICITKMDL 120 IEDQDTEDTI QAYAEDYRNI GYDVYLTSSK DQDSLADIIP HFQDKTTVFA GQSGVGKSSL 180 LNAISPELGL RTNEISEHLG RGKHTTRHVE LIHTSGGLVA DTPGFSSLEF TDIEEEELGY 240 TFPDIREKSS SCKFRGCLHL KEPKCAVKQA VEDGELKQYR YDHYVEFMTE IKDRKPRY 298 |
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