ETTA_ECOLI
ID ETTA_ECOLI Reviewed; 555 AA.
AC P0A9W3; P37797; Q2M5S6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Energy-dependent translational throttle protein EttA {ECO:0000255|HAMAP-Rule:MF_00847, ECO:0000303|PubMed:24389465};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00847, ECO:0000269|PubMed:24389465};
DE AltName: Full=Translational regulatory factor EttA {ECO:0000255|HAMAP-Rule:MF_00847, ECO:0000303|PubMed:24500425};
GN Name=ettA {ECO:0000255|HAMAP-Rule:MF_00847, ECO:0000303|PubMed:24389465};
GN Synonyms=yjjK; OrderedLocusNames=b4391, JW4354;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP C-TERMINUS.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX PubMed=1938883; DOI=10.1128/jb.173.21.6773-6782.1991;
RA Engel H., Kazemier B., Keck W.;
RT "Murein-metabolizing enzymes from Escherichia coli: sequence analysis and
RT controlled overexpression of the slt gene, which encodes the soluble lytic
RT transglycosylase.";
RL J. Bacteriol. 173:6773-6782(1991).
RN [5]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [7]
RP FAMILY, AND MUTAGENESIS OF GLU-188 AND GLU-470.
RC STRAIN=K12 / BW25113;
RX PubMed=30597160; DOI=10.1016/j.jmb.2018.12.013;
RA Murina V., Kasari M., Takada H., Hinnu M., Saha C.K., Grimshaw J.W.,
RA Seki T., Reith M., Putrins M., Tenson T., Strahl H., Hauryliuk V.,
RA Atkinson G.C.;
RT "ABCF ATPases involved in protein synthesis, ribosome assembly and
RT antibiotic resistance: structural and functional diversification across the
RT tree of life.";
RL J. Mol. Biol. 431:3568-3590(2019).
RN [8] {ECO:0007744|PDB:4FIN}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, INDUCTION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLU-188 AND GLU-470.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24389466; DOI=10.1038/nsmb.2740;
RA Boel G., Smith P.C., Ning W., Englander M.T., Chen B., Hashem Y.,
RA Testa A.J., Fischer J.J., Wieden H.J., Frank J., Gonzalez R.L. Jr.,
RA Hunt J.F.;
RT "The ABC-F protein EttA gates ribosome entry into the translation
RT elongation cycle.";
RL Nat. Struct. Mol. Biol. 21:143-151(2014).
RN [9] {ECO:0007744|PDB:3J5S}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.5 ANGSTROMS) IN COMPLEX WITH 70S
RP RIBOSOMES, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF GLU-188 AND
RP GLU-470.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24389465; DOI=10.1038/nsmb.2741;
RA Chen B., Boel G., Hashem Y., Ning W., Fei J., Wang C., Gonzalez R.L. Jr.,
RA Hunt J.F., Frank J.;
RT "EttA regulates translation by binding the ribosomal E site and restricting
RT ribosome-tRNA dynamics.";
RL Nat. Struct. Mol. Biol. 21:152-159(2014).
RN [10]
RP COMMENT.
RX PubMed=24500425; DOI=10.1038/nsmb.2765;
RA Fredrick K., Ibba M.;
RT "The ABCs of the ribosome.";
RL Nat. Struct. Mol. Biol. 21:115-116(2014).
CC -!- FUNCTION: A translation factor that gates the progression of the 70S
CC ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site)
CC into the translation elongation cycle by using a mechanism sensitive to
CC the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates
CC the state of the translating ribosome during subunit translocation.
CC Stimulates dipeptide bond synthesis in the presence of ATP (cell in
CC high energy state), but inhibits dipeptide synthesis in the presence of
CC ADP (cell in low energy state), and thus may control translation in
CC response to changing ATP levels (including during stationary phase).
CC Following ATP hydrolysis is probably released allowing the ribosome to
CC enter the elongation phase. ATPase activity is stimulated in the
CC presence of ribosomes. Its specificity for the IC may be conferred by
CC its recognition of features unique to tRNA(fMet).
CC {ECO:0000269|PubMed:24389465, ECO:0000269|PubMed:24389466}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00847, ECO:0000269|PubMed:24389465};
CC -!- SUBUNIT: Monomer at concentrations found in vivo, exists in a slowly
CC reversible monomer-homodimer equilibrium. Probably contacts ribosomal
CC proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P-site
CC containing tRNA(fMet). {ECO:0000269|PubMed:24389465,
CC ECO:0000269|PubMed:24389466}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00847,
CC ECO:0000269|PubMed:24389466}. Note=Associates with ribosomes and
CC polysomes. {ECO:0000255|HAMAP-Rule:MF_00847}.
CC -!- INDUCTION: Constitutively expressed, increases in stationary phase (at
CC protein level). {ECO:0000269|PubMed:24389466}.
CC -!- DOMAIN: The arm domain (residues 95-139) is inserted in the first ABC
CC transporter domain. Its deletion abrogates the growth arrest and
CC translation inhibition effect of the double Q-188/Q-470 mutation. When
CC deleted impairs fitness in long-term (up to 6 days) growth in
CC stationary phase (PubMed:24389466). Probably contacts ribosomal protein
CC L1 (PubMed:24389465). {ECO:0000269|PubMed:24389465,
CC ECO:0000269|PubMed:24389466}.
CC -!- DOMAIN: The P-site tRNA interaction motif (PtIM domain, residues 242-
CC 322) probably interacts with the P-site tRNA(fMet) as well as the 23S
CC rRNA. {ECO:0000269|PubMed:24389465}.
CC -!- DISRUPTION PHENOTYPE: Not essential it can be disrupted, its absence
CC impairs fitness in long-term (up to 6 days) growth in stationary phase.
CC {ECO:0000269|PubMed:24389466}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC Translational throttle EttA subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00847, ECO:0000303|PubMed:30597160}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97287.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=M69185; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97287.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC77344.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78380.1; -; Genomic_DNA.
DR EMBL; M69185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; F65254; F65254.
DR RefSeq; NP_418808.1; NC_000913.3.
DR RefSeq; WP_000046749.1; NZ_STEB01000033.1.
DR PDB; 3J5S; EM; 7.50 A; D=1-555.
DR PDB; 4FIN; X-ray; 2.40 A; A/B=1-555.
DR PDBsum; 3J5S; -.
DR PDBsum; 4FIN; -.
DR AlphaFoldDB; P0A9W3; -.
DR SMR; P0A9W3; -.
DR BioGRID; 4260798; 21.
DR BioGRID; 853186; 1.
DR DIP; DIP-48138N; -.
DR IntAct; P0A9W3; 13.
DR STRING; 511145.b4391; -.
DR jPOST; P0A9W3; -.
DR PaxDb; P0A9W3; -.
DR PRIDE; P0A9W3; -.
DR EnsemblBacteria; AAC77344; AAC77344; b4391.
DR EnsemblBacteria; BAE78380; BAE78380; BAE78380.
DR GeneID; 66671721; -.
DR GeneID; 948909; -.
DR KEGG; ecj:JW4354; -.
DR KEGG; eco:b4391; -.
DR PATRIC; fig|1411691.4.peg.2293; -.
DR EchoBASE; EB2247; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR InParanoid; P0A9W3; -.
DR OMA; ISYKPQY; -.
DR PhylomeDB; P0A9W3; -.
DR BioCyc; EcoCyc:YJJK-MON; -.
DR PRO; PR:P0A9W3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0043022; F:ribosome binding; IMP:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045900; P:negative regulation of translational elongation; IDA:EcoCyc.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00847; EttA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR022374; EttA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43858; PTHR43858; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03719; ABC_ABC_ChvD; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..555
FT /note="Energy-dependent translational throttle protein
FT EttA"
FT /id="PRO_0000093191"
FT DOMAIN 6..259
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT DOMAIN 324..550
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT REGION 95..139
FT /note="Arm"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847,
FT ECO:0000269|PubMed:24389465"
FT REGION 242..322
FT /note="PtIM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847,
FT ECO:0000269|PubMed:24389465"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT MUTAGEN 188
FT /note="E->Q: Arrests growth, inhibits tripeptide but not
FT dipeptide formation, stably binds 70S ribosomes, probably
FT locked in an ATP-bound form as it should not have ATPase
FT activity, 47-fold decrease in translation; when associated
FT with Q-470 (called EQ2)."
FT /evidence="ECO:0000269|PubMed:24389465,
FT ECO:0000269|PubMed:24389466, ECO:0000269|PubMed:30597160"
FT MUTAGEN 470
FT /note="E->Q: Arrests growth, inhibits tripeptide but not
FT dipeptide formation, stably binds 70S ribosomes, probably
FT locked in an ATP-bound form as it should not have ATPase
FT activity, 47-fold decrease in translation; when associated
FT with Q-188 (EQ2)."
FT /evidence="ECO:0000269|PubMed:24389465,
FT ECO:0000269|PubMed:24389466, ECO:0000269|PubMed:30597160"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:4FIN"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 19..29
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:4FIN"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:4FIN"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 244..276
FT /evidence="ECO:0007829|PDB:4FIN"
FT TURN 287..293
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 324..333
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 336..346
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:4FIN"
FT TURN 471..474
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 477..489
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 501..507
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:4FIN"
FT HELIX 527..538
FT /evidence="ECO:0007829|PDB:4FIN"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:4FIN"
SQ SEQUENCE 555 AA; 62443 MW; 444C7A3E2492D978 CRC64;
MAQFVYTMHR VGKVVPPKRH ILKNISLSFF PGAKIGVLGL NGAGKSTLLR IMAGIDKDIE
GEARPQPDIK IGYLPQEPQL NPEHTVRESI EEAVSEVVNA LKRLDEVYAL YADPDADFDK
LAAEQGRLEE IIQAHDGHNL NVQLERAADA LRLPDWDAKI ANLSGGERRR VALCRLLLEK
PDMLLLDEPT NHLDAESVAW LERFLHDFEG TVVAITHDRY FLDNVAGWIL ELDRGEGIPW
EGNYSSWLEQ KDQRLAQEAS QEAARRKSIE KELEWVRQGT KGRQSKGKAR LARFEELNST
EYQKRNETNE LFIPPGPRLG DKVLEVSNLR KSYGDRLLID DLSFSIPKGA IVGIIGPNGA
GKSTLFRMIS GQEQPDSGTI TLGETVKLAS VDQFRDSMDN SKTVWEEVSG GLDIMKIGNT
EMPSRAYVGR FNFKGVDQGK RVGELSGGER GRLHLAKLLQ VGGNMLLLDE PTNDLDIETL
RALENALLEF PGCAMVISHD RWFLDRIATH ILDYQDEGKV EFFEGNFTEY EEYKKRTLGA
DALEPKRIKY KRIAK
