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Protein

Energy-dependent translational throttle protein EttA

Gene

ettA

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

Functioni

A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E site where it modulates the state of the translating ribosome during subunit translocation. Stimulates dipeptide bond synthesis in the presence of ATP (cell in high energy state), but inhibits dipeptide synthesis in the presence of ADP (cell in low energy state), and thus may control translation in response to changing ATP levels (including during stationary phase). Following ATP hydrolysis is probably released allowing the ribosome to enter the elongation phase. Its specificity for the IC may be conferred by its recognition of features unique to tRNA(fMet).2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 468ATP 1PROSITE-ProRule annotation
Nucleotide bindingi356 – 3638ATP 2PROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • ribosome binding Source: EcoCyc
  • rRNA binding Source: UniProtKB-KW
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • negative regulation of translational elongation Source: EcoCyc
  • translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:YJJK-MONOMER.
ECOL316407:JW4354-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Energy-dependent translational throttle protein EttA
Alternative name(s):
Translational regulatory factor EttA
Gene namesi
Name:ettA
Synonyms:yjjK
Ordered Locus Names:b4391, JW4354
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12343. ettA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Not essential it can be disrupted, its absence impairs fitness in long-term (up to 6 days) growth in stationary phase.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881E → Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity; when associated with Q-470. 2 Publications
Mutagenesisi470 – 4701E → Q: Arrests growth, inhibits tripeptide but not dipeptide formation, stably binds 70S ribosomes, probably locked in an ATP-bound form as it should not have ATPase activity; when associated with Q-188. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 555554Energy-dependent translational throttle protein EttAPRO_0000093191Add
BLAST

Proteomic databases

EPDiP0A9W3.
PaxDbiP0A9W3.
PRIDEiP0A9W3.

Expressioni

Inductioni

Constitutively expressed, increases in stationary phase (at protein level).1 Publication

Interactioni

Subunit structurei

Monomer at concentrations found in vivo, exists in a slowly reversible monomer-homodimer equilibrium. Probably contacts ribosomal proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P site containing tRNA(fMet).2 Publications

Protein-protein interaction databases

BioGridi4260798. 5 interactions.
DIPiDIP-48138N.
IntActiP0A9W3. 8 interactions.
MINTiMINT-1222078.
STRINGi511145.b4391.

Structurei

Secondary structure

1
555
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1511Combined sources
Turni16 – 183Combined sources
Beta strandi19 – 2911Combined sources
Beta strandi34 – 396Combined sources
Helixi45 – 528Combined sources
Beta strandi60 – 656Combined sources
Beta strandi71 – 744Combined sources
Helixi86 – 938Combined sources
Helixi95 – 11016Combined sources
Helixi118 – 13114Combined sources
Helixi141 – 15010Combined sources
Turni160 – 1623Combined sources
Helixi165 – 17915Combined sources
Beta strandi182 – 1887Combined sources
Turni189 – 1924Combined sources
Helixi195 – 20713Combined sources
Beta strandi209 – 2157Combined sources
Helixi219 – 2246Combined sources
Beta strandi227 – 2359Combined sources
Beta strandi237 – 2426Combined sources
Helixi244 – 27633Combined sources
Turni287 – 2937Combined sources
Helixi294 – 2974Combined sources
Helixi300 – 3056Combined sources
Helixi306 – 3083Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi324 – 33310Combined sources
Beta strandi336 – 34611Combined sources
Beta strandi351 – 3555Combined sources
Helixi362 – 3698Combined sources
Beta strandi376 – 3827Combined sources
Beta strandi388 – 3914Combined sources
Helixi404 – 4096Combined sources
Beta strandi413 – 4175Combined sources
Beta strandi420 – 4234Combined sources
Helixi424 – 4296Combined sources
Helixi435 – 4373Combined sources
Helixi442 – 4443Combined sources
Helixi447 – 45812Combined sources
Helixi459 – 4613Combined sources
Beta strandi464 – 4707Combined sources
Turni471 – 4744Combined sources
Helixi477 – 48913Combined sources
Beta strandi491 – 4977Combined sources
Helixi501 – 5077Combined sources
Beta strandi509 – 5146Combined sources
Beta strandi520 – 5256Combined sources
Helixi527 – 53812Combined sources
Beta strandi542 – 5443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J5Selectron microscopy7.50D1-555[»]
4FINX-ray2.40A/B1-555[»]
ProteinModelPortaliP0A9W3.
SMRiP0A9W3. Positions 2-555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 259254ABC transporter 1PROSITE-ProRule annotationAdd
BLAST
Domaini324 – 550227ABC transporter 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 13945ArmAdd
BLAST
Regioni242 – 32281PtIMAdd
BLAST

Domaini

The arm domain (residues 95-139) is inserted in the first ABC transporter domain. Its deletion abrogates the growth arrest and translation inhibition effect of the double Q-188/Q-470 mutation. When deleted impairs fitness in long-term (up to 6 days) growth in stationary phase (PubMed:24389466). Probably contacts ribosomal protein L1 (PubMed:24389465).2 Publications
The P-site tRNA interaction motif (PtIM domain, residues 242-322) probably interacts with the P site tRNA(fMet) as well as the 23S rRNA.

Sequence similaritiesi

Contains 2 ABC transporter domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105C5H. Bacteria.
COG0488. LUCA.
HOGENOMiHOG000271639.
InParanoidiP0A9W3.
OMAiKVIEFQD.
PhylomeDBiP0A9W3.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR003593. AAA+_ATPase.
IPR022374. ABC_ATP-bd_ChvD.
IPR032781. ABC_tran_Xtn.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00005. ABC_tran. 2 hits.
PF12848. ABC_tran_Xtn. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR03719. ABC_ABC_ChvD. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A9W3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQFVYTMHR VGKVVPPKRH ILKNISLSFF PGAKIGVLGL NGAGKSTLLR
60 70 80 90 100
IMAGIDKDIE GEARPQPDIK IGYLPQEPQL NPEHTVRESI EEAVSEVVNA
110 120 130 140 150
LKRLDEVYAL YADPDADFDK LAAEQGRLEE IIQAHDGHNL NVQLERAADA
160 170 180 190 200
LRLPDWDAKI ANLSGGERRR VALCRLLLEK PDMLLLDEPT NHLDAESVAW
210 220 230 240 250
LERFLHDFEG TVVAITHDRY FLDNVAGWIL ELDRGEGIPW EGNYSSWLEQ
260 270 280 290 300
KDQRLAQEAS QEAARRKSIE KELEWVRQGT KGRQSKGKAR LARFEELNST
310 320 330 340 350
EYQKRNETNE LFIPPGPRLG DKVLEVSNLR KSYGDRLLID DLSFSIPKGA
360 370 380 390 400
IVGIIGPNGA GKSTLFRMIS GQEQPDSGTI TLGETVKLAS VDQFRDSMDN
410 420 430 440 450
SKTVWEEVSG GLDIMKIGNT EMPSRAYVGR FNFKGVDQGK RVGELSGGER
460 470 480 490 500
GRLHLAKLLQ VGGNMLLLDE PTNDLDIETL RALENALLEF PGCAMVISHD
510 520 530 540 550
RWFLDRIATH ILDYQDEGKV EFFEGNFTEY EEYKKRTLGA DALEPKRIKY

KRIAK
Length:555
Mass (Da):62,443
Last modified:January 23, 2007 - v2
Checksum:i444C7A3E2492D978
GO

Sequence cautioni

The sequence AAA97287 differs from that shown. Reason: Frameshift at position 541. Curated
The sequence M69185 differs from that shown. Reason: Frameshift at position 49. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97287.1. Frameshift.
U00096 Genomic DNA. Translation: AAC77344.1.
AP009048 Genomic DNA. Translation: BAE78380.1.
M69185 Genomic DNA. No translation available.
PIRiF65254.
RefSeqiNP_418808.1. NC_000913.3.
WP_000046749.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77344; AAC77344; b4391.
BAE78380; BAE78380; BAE78380.
GeneIDi948909.
KEGGiecj:JW4354.
eco:b4391.
PATRICi32124400. VBIEscCol129921_4540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97287.1. Frameshift.
U00096 Genomic DNA. Translation: AAC77344.1.
AP009048 Genomic DNA. Translation: BAE78380.1.
M69185 Genomic DNA. No translation available.
PIRiF65254.
RefSeqiNP_418808.1. NC_000913.3.
WP_000046749.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J5Selectron microscopy7.50D1-555[»]
4FINX-ray2.40A/B1-555[»]
ProteinModelPortaliP0A9W3.
SMRiP0A9W3. Positions 2-555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260798. 5 interactions.
DIPiDIP-48138N.
IntActiP0A9W3. 8 interactions.
MINTiMINT-1222078.
STRINGi511145.b4391.

Proteomic databases

EPDiP0A9W3.
PaxDbiP0A9W3.
PRIDEiP0A9W3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77344; AAC77344; b4391.
BAE78380; BAE78380; BAE78380.
GeneIDi948909.
KEGGiecj:JW4354.
eco:b4391.
PATRICi32124400. VBIEscCol129921_4540.

Organism-specific databases

EchoBASEiEB2247.
EcoGeneiEG12343. ettA.

Phylogenomic databases

eggNOGiENOG4105C5H. Bacteria.
COG0488. LUCA.
HOGENOMiHOG000271639.
InParanoidiP0A9W3.
OMAiKVIEFQD.
PhylomeDBiP0A9W3.

Enzyme and pathway databases

BioCyciEcoCyc:YJJK-MONOMER.
ECOL316407:JW4354-MONOMER.

Miscellaneous databases

PROiP0A9W3.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR003593. AAA+_ATPase.
IPR022374. ABC_ATP-bd_ChvD.
IPR032781. ABC_tran_Xtn.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00005. ABC_tran. 2 hits.
PF12848. ABC_tran_Xtn. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR03719. ABC_ABC_ChvD. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiETTA_ECOLI
AccessioniPrimary (citable) accession number: P0A9W3
Secondary accession number(s): P37797, Q2M5S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.