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Protein

GTPase Era

Gene

era

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Enzyme regulationi

GTPase is competitively inhibited by GDP but not by ADP, ATP, CTP or UTP.1 Publication

Kineticsi

  1. KM=15.4 µM for GTP (for His-tagged protein at pH 8.0, 5 mM MgCl2)2 Publications
  2. KM=9.0 µM for GTP (for overexpressed protein at pH 8.0, 5 mM MgCl2)2 Publications

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi15 – 22GTP8
    Nucleotide bindingi62 – 66GTP5
    Nucleotide bindingi124 – 127GTP4

    GO - Molecular functioni

    • GTPase activity Source: UniProtKB
    • GTP binding Source: UniProtKB
    • ribosomal small subunit binding Source: UniProtKB
    • small ribosomal subunit rRNA binding Source: UniProtKB

    GO - Biological processi

    • protein phosphorylation Source: UniProtKB
    • ribosomal small subunit assembly Source: GO_Central
    • ribosomal small subunit biogenesis Source: UniProtKB
    Complete GO annotation...

    Keywords - Biological processi

    Ribosome biogenesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10270-MONOMER.
    ECOL316407:JW2550-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTPase Era
    Short name:
    ERA
    Alternative name(s):
    GTP-binding protein Era
    Gene namesi
    Name:era
    Synonyms:rbaA, sdgE
    Ordered Locus Names:b2566, JW2550
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10270. era.

    Subcellular locationi

    • Cytoplasm 1 Publication
    • Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

    • Note: Binding is GDP or GTP-dependent, slightly more protein is bound in the presence of GTP than GDP.

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: EcoCyc
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Lethality. In the presence of 1% protein cells grow extremely slowly and are blocked at the predivisional two-cell stage of the cell cycle. In the absence of Era and Rnc there is an additional defect in chromosome partitioning. In depletion experiments cells grow normally for 2 hours when protein levels fall. After 4 hours 16S rRNA levels decrease with a concomitant rise in the 17S precursor rRNA molecule (extra sequences at both the 5' and 3' end compared to mature 16S rRNA) and a loss of 70S ribosome assembly.3 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi8C → A in era770; 20-fold reduction in GTP-binding. Confers growth sensitivity at 42 degrees Celsius; when associated with an unpublished 22 residue replacement in the C-terminus. 1 Publication1
    Mutagenesisi17P → R in era1; suppresses a number of temperature-sensitive mutations affecting cell cycle. 2 Publications1
    Mutagenesisi17P → V: Confers sensitivity to cold. 2 Publications1
    Mutagenesisi26N → S: Confers sensitivity to cold; overexpression does not suppress an rbfA disruption. 1 Publication1
    Mutagenesisi39 – 49KAQTTRHRIVG → R in Era-de; does not complement a disruption mutant, overexpression in a wt cells inhibits growth. Binds GTP poorly, Km for GTP increases 5-fold, Vmax for GTPase is 55% that of wt. Does not autophosphorylate. Complements cold-sensitivity and 16S rRNA processing in an rbfA disruption mutant. Add BLAST11
    Mutagenesisi42 – 43TT → AA: Does not complement a disruption mutant, Km for GTP increases 12-fold, Vmax for GTPase is 49% that of wt. Overexpression partially suppresses an rbfA disruption. 2 Publications2
    Mutagenesisi156A → D: Confers sensitivity to cold; overexpression partially suppresses an rbfA disruption. 1 Publication1
    Mutagenesisi200E → K: Confers sensitivity to cold, cells do not divide properly but do replicate DNA and segregate nucleoids normally. 16S rRNA processing is decreased, ribosome assembly is defective. Suppressed by overexpression of RsmA. Overexpression does not suppress an rbfA disruption, while at 37 degrees Celsius the rbfA/era E220K mutant grows very poorly, a dominant-negative effect. This mutant still binds 30S ribosomes. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001800122 – 301GTPase EraAdd BLAST300

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei36Phosphothreonine; by autocatalysis1 Publication1
    Modified residuei37Phosphoserine; by autocatalysis1 Publication1

    Post-translational modificationi

    Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP06616.
    PRIDEiP06616.

    PTM databases

    iPTMnetiP06616.

    Expressioni

    Inductioni

    Expression increases as the growth rate increases. Encoded in the rnc-era-recO operon.1 Publication

    Interactioni

    Subunit structurei

    Monomer. Binds both 16S rRNA and 30S ribosomal subunits; binding is inhibited by GDP and GTP. Binds to MazG; GDP-bound Era binds more tightly to MazG than GTP-bound Era.2 Publications

    Protein-protein interaction databases

    BioGridi4263220. 444 interactors.
    DIPiDIP-9521N.
    IntActiP06616. 28 interactors.
    MINTiMINT-1248282.
    STRINGi511145.b2566.

    Structurei

    Secondary structure

    1301
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 14Combined sources8
    Beta strandi16 – 20Combined sources5
    Helixi21 – 29Combined sources9
    Beta strandi32 – 35Combined sources4
    Beta strandi47 – 53Combined sources7
    Beta strandi56 – 65Combined sources10
    Helixi68 – 78Combined sources11
    Beta strandi89 – 97Combined sources9
    Helixi103 – 113Combined sources11
    Beta strandi114 – 117Combined sources4
    Beta strandi119 – 125Combined sources7
    Turni126 – 128Combined sources3
    Helixi132 – 143Combined sources12
    Beta strandi149 – 153Combined sources5
    Turni156 – 161Combined sources6
    Helixi162 – 170Combined sources9
    Helixi190 – 206Combined sources17
    Helixi207 – 209Combined sources3
    Beta strandi214 – 222Combined sources9
    Beta strandi228 – 239Combined sources12
    Helixi240 – 247Combined sources8
    Helixi249 – 251Combined sources3
    Helixi252 – 268Combined sources17
    Beta strandi273 – 281Combined sources9
    Helixi287 – 292Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EGAX-ray2.40A/B1-301[»]
    3IEUX-ray2.80A/B1-301[»]
    ProteinModelPortaliP06616.
    SMRiP06616.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06616.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini7 – 175Era-type GAdd BLAST169
    Domaini206 – 283KH type-2Add BLAST78

    Sequence similaritiesi

    Contains 1 KH type-2 domain.Curated

    Phylogenomic databases

    eggNOGiENOG4105CWT. Bacteria.
    COG1159. LUCA.
    HOGENOMiHOG000245597.
    InParanoidiP06616.
    KOiK03595.
    OMAiKVAKDWQ.
    PhylomeDBiP06616.

    Family and domain databases

    CDDicd04163. Era. 1 hit.
    Gene3Di3.30.300.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_00367. GTPase_Era. 1 hit.
    InterProiIPR030388. G_ERA_dom.
    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.
    [Graphical view]
    PfamiPF07650. KH_2. 1 hit.
    PF01926. MMR_HSR1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF54814. SSF54814. 1 hit.
    TIGRFAMsiTIGR00436. era. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEiPS51713. G_ERA. 1 hit.
    PS50823. KH_TYPE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06616-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSIDKSYCGF IAIVGRPNVG KSTLLNKLLG QKISITSRKA QTTRHRIVGI
    60 70 80 90 100
    HTEGAYQAIY VDTPGLHMEE KRAINRLMNK AASSSIGDVE LVIFVVEGTR
    110 120 130 140 150
    WTPDDEMVLN KLREGKAPVI LAVNKVDNVQ EKADLLPHLQ FLASQMNFLD
    160 170 180 190 200
    IVPISAETGL NVDTIAAIVR KHLPEATHHF PEDYITDRSQ RFMASEIIRE
    210 220 230 240 250
    KLMRFLGAEL PYSVTVEIER FVSNERGGYD INGLILVERE GQKKMVIGNK
    260 270 280 290 300
    GAKIKTIGIE ARKDMQEMFE APVHLELWVK VKSGWADDER ALRSLGYVDD

    L
    Length:301
    Mass (Da):33,810
    Last modified:February 1, 1994 - v2
    Checksum:i53F275F07BDAE593
    GO

    Mass spectrometryi

    Molecular mass is 33682±5 Da from positions 2 - 301. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M14658 Unassigned DNA. Translation: AAA03242.1.
    D64044 Genomic DNA. Translation: BAA10913.1.
    U36841 Genomic DNA. Translation: AAA79828.1.
    U00096 Genomic DNA. Translation: AAC75619.1.
    AP009048 Genomic DNA. Translation: BAE76742.1.
    X02673 Genomic DNA. Translation: CAA26505.1.
    PIRiS44713. RGECGT.
    RefSeqiNP_417061.1. NC_000913.3.
    WP_000020749.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75619; AAC75619; b2566.
    BAE76742; BAE76742; BAE76742.
    GeneIDi947036.
    KEGGiecj:JW2550.
    eco:b2566.
    PATRICi32120531. VBIEscCol129921_2668.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M14658 Unassigned DNA. Translation: AAA03242.1.
    D64044 Genomic DNA. Translation: BAA10913.1.
    U36841 Genomic DNA. Translation: AAA79828.1.
    U00096 Genomic DNA. Translation: AAC75619.1.
    AP009048 Genomic DNA. Translation: BAE76742.1.
    X02673 Genomic DNA. Translation: CAA26505.1.
    PIRiS44713. RGECGT.
    RefSeqiNP_417061.1. NC_000913.3.
    WP_000020749.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EGAX-ray2.40A/B1-301[»]
    3IEUX-ray2.80A/B1-301[»]
    ProteinModelPortaliP06616.
    SMRiP06616.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263220. 444 interactors.
    DIPiDIP-9521N.
    IntActiP06616. 28 interactors.
    MINTiMINT-1248282.
    STRINGi511145.b2566.

    PTM databases

    iPTMnetiP06616.

    Proteomic databases

    PaxDbiP06616.
    PRIDEiP06616.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75619; AAC75619; b2566.
    BAE76742; BAE76742; BAE76742.
    GeneIDi947036.
    KEGGiecj:JW2550.
    eco:b2566.
    PATRICi32120531. VBIEscCol129921_2668.

    Organism-specific databases

    EchoBASEiEB0266.
    EcoGeneiEG10270. era.

    Phylogenomic databases

    eggNOGiENOG4105CWT. Bacteria.
    COG1159. LUCA.
    HOGENOMiHOG000245597.
    InParanoidiP06616.
    KOiK03595.
    OMAiKVAKDWQ.
    PhylomeDBiP06616.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10270-MONOMER.
    ECOL316407:JW2550-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP06616.
    PROiP06616.

    Family and domain databases

    CDDicd04163. Era. 1 hit.
    Gene3Di3.30.300.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_00367. GTPase_Era. 1 hit.
    InterProiIPR030388. G_ERA_dom.
    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.
    [Graphical view]
    PfamiPF07650. KH_2. 1 hit.
    PF01926. MMR_HSR1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF54814. SSF54814. 1 hit.
    TIGRFAMsiTIGR00436. era. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEiPS51713. G_ERA. 1 hit.
    PS50823. KH_TYPE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiERA_ECOLI
    AccessioniPrimary (citable) accession number: P06616
    Secondary accession number(s): Q2MAG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: February 1, 1994
    Last modified: November 2, 2016
    This is version 169 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    When overexpressed partially suppresses the slow growth and decreased 70S ribosome phenotype of an rsgA knockout; RsgA may be involved in 30S ribosomal subunit biogenesis. When overexpressed partially suppresses the ribosome assembly defects and cold-sensitivity of an rbfA knockout; an era mutant missing residues 40-49 fully suppresses these phenotypes. RbfA plays a role in 30S ribosomal subunit maturation. Overexpression is not able to suppress a rimM disruption phenotype nor a C23U mutation in 16S rRNA. Also suppresses temperature-sensitive mutations in DNA primase.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.