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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi39 – 46ATP 1PROSITE-ProRule annotation8
Nucleotide bindingi356 – 363ATP 2PROSITE-ProRule annotation8

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi188E → 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 Publications1
Mutagenesisi470E → 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 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000931912 – 555Energy-dependent translational throttle protein EttAAdd BLAST554

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 interactors.
DIPiDIP-48138N.
IntActiP0A9W3. 8 interactors.
MINTiMINT-1222078.
STRINGi511145.b4391.

Structurei

Secondary structure

1555
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 15Combined sources11
Turni16 – 18Combined sources3
Beta strandi19 – 29Combined sources11
Beta strandi34 – 39Combined sources6
Helixi45 – 52Combined sources8
Beta strandi60 – 65Combined sources6
Beta strandi71 – 74Combined sources4
Helixi86 – 93Combined sources8
Helixi95 – 110Combined sources16
Helixi118 – 131Combined sources14
Helixi141 – 150Combined sources10
Turni160 – 162Combined sources3
Helixi165 – 179Combined sources15
Beta strandi182 – 188Combined sources7
Turni189 – 192Combined sources4
Helixi195 – 207Combined sources13
Beta strandi209 – 215Combined sources7
Helixi219 – 224Combined sources6
Beta strandi227 – 235Combined sources9
Beta strandi237 – 242Combined sources6
Helixi244 – 276Combined sources33
Turni287 – 293Combined sources7
Helixi294 – 297Combined sources4
Helixi300 – 305Combined sources6
Helixi306 – 308Combined sources3
Beta strandi309 – 311Combined sources3
Beta strandi324 – 333Combined sources10
Beta strandi336 – 346Combined sources11
Beta strandi351 – 355Combined sources5
Helixi362 – 369Combined sources8
Beta strandi376 – 382Combined sources7
Beta strandi388 – 391Combined sources4
Helixi404 – 409Combined sources6
Beta strandi413 – 417Combined sources5
Beta strandi420 – 423Combined sources4
Helixi424 – 429Combined sources6
Helixi435 – 437Combined sources3
Helixi442 – 444Combined sources3
Helixi447 – 458Combined sources12
Helixi459 – 461Combined sources3
Beta strandi464 – 470Combined sources7
Turni471 – 474Combined sources4
Helixi477 – 489Combined sources13
Beta strandi491 – 497Combined sources7
Helixi501 – 507Combined sources7
Beta strandi509 – 514Combined sources6
Beta strandi520 – 525Combined sources6
Helixi527 – 538Combined sources12
Beta strandi542 – 544Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 259ABC transporter 1PROSITE-ProRule annotationAdd BLAST254
Domaini324 – 550ABC transporter 2PROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni95 – 139ArmAdd BLAST45
Regioni242 – 322PtIMAdd BLAST81

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J5Selectron microscopy7.50D1-555[»]
4FINX-ray2.40A/B1-555[»]
ProteinModelPortaliP0A9W3.
SMRiP0A9W3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260798. 5 interactors.
DIPiDIP-48138N.
IntActiP0A9W3. 8 interactors.
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: November 2, 2016
This is version 92 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.