UniProt Accession

 ERA_ECOLI; P06616; Q2MAG4 

Genbank Protein ID

 M14658; D64044; U36841; U00096; AP009048; X02673 

Genbank Nucleotide ID

 AAA03242.1; BAA10913.1; AAA79828.1; AAC75619.1; BAE76742.1; CAA26505.1 

Protein Name

 GTPase Era 

Protein Synonyms/Alias

 ERA; GTP-binding protein Era 

Gene Name

 era 

Gene Synonyms/Alias

 rbaA; sdgE; b2566; JW2550 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
27	GKSTLLNKLLGQKIS	acetylation	[1]
71	PGLHMEEKRAINRLM	acetylation	[1]
111	DDEMVLNKLREGKAP	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 20 125 G.
 DOMAIN 206 283 KH type-2.
 NP_BIND 15 22 GTP.
 NP_BIND 62 66 GTP.
 NP_BIND 124 127 GTP.
 MOD_RES 36 36 Phosphothreonine; by autocatalysis.
 MOD_RES 37 37 Phosphoserine; by autocatalysis.  

Keyword

 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 301 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IDA:UniProtKB.
 GO:0003924; F:GTPase activity; IDA:UniProtKB.
 GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
 GO:0070181; F:SSU rRNA binding; IDA:UniProtKB.
 GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
 GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB. 

Interpro

 IPR005662; GTP-bd_Era.
 IPR006073; GTP_binding_domain.
 IPR015946; KH_dom-like_a/b.
 IPR004044; KH_dom_type_2.
 IPR009019; KH_prok-type.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom. 

Pfam

 PF07650; KH_2
 PF01926; MMR_HSR1 

SMART

  

PROSITE

 PS50823; KH_TYPE_2 

PRINTS