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UniProtKB - P06616 (ERA_ECOLI)

Entry version 202 (23 Feb 2022)
Sequence version 2 (01 Feb 1994)
Previous versions | rss
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Protein

GTPase Era

Gene

era

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late assembly stage of the 30S ribosomal subunit. 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 (PubMed:16825789).

Binds to the pre-30S ribosomal subunit through several stages of protein assembly (PubMed:20188109).

4 Publications

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 (PubMed:18223068). When overexpressed partially suppresses the 30S ribosomal subunit assembly defects and cold-sensitivity of an rbfA knockout; an era mutant missing residues 39-49 fully suppresses these phenotypes (PubMed:12753192). 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 (PubMed:9093842).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi15 – 22GTP8
Nucleotide bindingi62 – 66GTP5
Nucleotide bindingi124 – 127GTP4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding, rRNA-binding
Biological processRibosome biogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10270-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P06616

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
GTPase Era
Short name:
ERA
Alternative name(s):
GTP-binding protein Era
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:era
Synonyms:rbaA, sdgE
Ordered Locus Names:b2566, JW2550
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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. 1 PublicationAdd 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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001800122 – 301GTPase EraAdd BLAST300

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei36Phosphothreonine; by autocatalysis1 Publication1
Modified residuei37Phosphoserine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06616

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P06616

PRoteomics IDEntifications database

More...PRIDEi		P06616

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06616

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Binds both 16S rRNA and 30S ribosomal subunits; binding is inhibited by GDP and GTP (PubMed:10094501). Bind preferentially to mature 30S ribosomal subunits over immature subunits in the presence of GMP-PNP (PubMed:27382067). Binds to MazG; GDP-bound Era binds more tightly to MazG than GTP-bound Era (PubMed:19706445).

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263220, 465 interactors
851375, 7 interactors

Database of interacting proteins

More...DIPi		DIP-9521N

Protein interaction database and analysis system

More...IntActi		P06616, 29 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2566

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06616

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06616

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 175Era-type GPROSITE-ProRule annotationAdd BLAST169
Domaini206 – 283KH type-2Add BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni15 – 22G1PROSITE-ProRule annotation8
Regioni41 – 45G2PROSITE-ProRule annotation5
Regioni62 – 65G3PROSITE-ProRule annotation4
Regioni124 – 127G4PROSITE-ProRule annotation4
Regioni154 – 156G5PROSITE-ProRule annotation3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family.PROSITE-ProRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1159, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_038009_1_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06616

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06616

Family and domain databases

Conserved Domains Database

More...CDDi		cd04163, Era, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.300.20, 1 hit
3.40.50.300, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00367, GTPase_Era, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR030388, G_ERA_dom
IPR006073, GTP-bd
IPR005662, GTP-bd_Era
IPR015946, KH_dom-like_a/b
IPR004044, KH_dom_type_2
IPR009019, KH_sf_prok-type
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom

The PANTHER Classification System

More...PANTHERi		PTHR42698, PTHR42698, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07650, KH_2, 1 hit
PF01926, MMR_HSR1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit
SSF54814, SSF54814, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00436, era, 1 hit
TIGR00231, small_GTP, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51713, G_ERA, 1 hit
PS50823, KH_TYPE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i53F275F07BDAE593
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 33682±5 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		S44713, RGECGT

NCBI Reference Sequences

More...RefSeqi		NP_417061.1, NC_000913.3
WP_000020749.1, NZ_STEB01000011.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75619; AAC75619; b2566
BAE76742; BAE76742; BAE76742

Database of genes from NCBI RefSeq genomes

More...GeneIDi		58391288
947036

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2550
eco:b2566

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4168

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_STEB01000011.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EGAX-ray2.40A/B1-301[»]
3IEUX-ray2.80A/B1-301[»]
SMRiP06616
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263220, 465 interactors
851375, 7 interactors
DIPiDIP-9521N
IntActiP06616, 29 interactors
STRINGi511145.b2566

PTM databases

iPTMnetiP06616

Proteomic databases

jPOSTiP06616
PaxDbiP06616
PRIDEiP06616

Genome annotation databases

EnsemblBacteriaiAAC75619; AAC75619; b2566
BAE76742; BAE76742; BAE76742
GeneIDi58391288
947036
KEGGiecj:JW2550
eco:b2566
PATRICifig|1411691.4.peg.4168

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0266

Phylogenomic databases

eggNOGiCOG1159, Bacteria
HOGENOMiCLU_038009_1_2_6
InParanoidiP06616
PhylomeDBiP06616

Enzyme and pathway databases

BioCyciEcoCyc:EG10270-MONOMER
SABIO-RKiP06616

Miscellaneous databases

EvolutionaryTraceiP06616

Protein Ontology

More...PROi		PR:P06616

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
InterProiView protein in InterPro
IPR030388, G_ERA_dom
IPR006073, GTP-bd
IPR005662, GTP-bd_Era
IPR015946, KH_dom-like_a/b
IPR004044, KH_dom_type_2
IPR009019, KH_sf_prok-type
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom
PANTHERiPTHR42698, PTHR42698, 1 hit
PfamiView protein in Pfam
PF07650, KH_2, 1 hit
PF01926, MMR_HSR1, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF54814, SSF54814, 1 hit
TIGRFAMsiTIGR00436, era, 1 hit
TIGR00231, small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51713, G_ERA, 1 hit
PS50823, KH_TYPE_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiERA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06616
Secondary accession number(s): Q2MAG4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1994
Last modified: February 23, 2022
This is version 202 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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