Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | GTPase Era |
Protein Synonyms/Alias | ERA |
Gene Name | era |
Gene Synonyms/Alias | rbaA, sdgE; OrderedLocusNames=b2566, JW2550 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 36 | LGQKISITSRKAQTT | T | NA | UniProt | 37 | GQKISITSRKAQTTR | S | NA | UniProt | |
Reference | |
Functional Description From UniProt | FUNCTION: An essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring on the order of seconds whereas hydrolysis occurs on the order of minutes. Plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing and 30S ribosomal subunit biogenesis. Its presence in the 30S subunit may prevent translation initiation. Seems to be critical for maintaining cell growth and cell divison rates; a dramatic reduction in Era protein levels temporarily arrests cell growth just before cytokinesis (at the predivisional two-cell stage) and delays cell division. Era mutant era1 suppresses some temperature- sensitive mutations that affect DNA replication and chromosome partitioning and segregation. The dominant-negative Era-de mutant which is missing residues in a putative effector region, is unable to complement the disruption mutant; upon overproduction it shows a significant decrease in cell viability and a synthetic lethal phenotype in the presence of acetate. Era function probably overlaps RbfA. Binds to the pre-30S subunit through several stages of protein assembly |
| MOD_RES 36 36 Phosphothreonine; by autocatalysis MOD_RES 37 37 Phosphoserine; by autocatalysis |
| 3D-structure; Cellinnermembrane; Cellmembrane; Completeproteome; Cytoplasm; Directproteinsequencing; GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein; Referenceproteome; Ribosomebiogenesis; RNA-binding; rRNA-binding |
Protein Sequence | MSIDKSYCGF IAIVGRPNVG KSTLLNKLLG QKISITSRKA QTTRHRIVGI HTEGAYQAIY 60 VDTPGLHMEE KRAINRLMNK AASSSIGDVE LVIFVVEGTR WTPDDEMVLN KLREGKAPVI 120 LAVNKVDNVQ EKADLLPHLQ FLASQMNFLD IVPISAETGL NVDTIAAIVR KHLPEATHHF 180 PEDYITDRSQ RFMASEIIRE KLMRFLGAEL PYSVTVEIER FVSNERGGYD INGLILVERE 240 GQKKMVIGNK GAKIKTIGIE ARKDMQEMFE APVHLELWVK VKSGWADDER ALRSLGYVDD 300 L 301 |
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