ETTA_ECOL6
ID ETTA_ECOL6 Reviewed; 555 AA.
AC A0A0H2VFI8;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Energy-dependent translational throttle protein EttA {ECO:0000255|HAMAP-Rule:MF_00847};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00847};
DE AltName: Full=Translational regulatory factor EttA {ECO:0000255|HAMAP-Rule:MF_00847};
GN Name=ettA {ECO:0000255|HAMAP-Rule:MF_00847}; Synonyms=yjjK;
GN OrderedLocusNames=c5478;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-188 AND GLU-470.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
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).
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. ATP
CC hydrolysis probably frees it from the ribosome, which can enter the
CC elongation phase. {ECO:0000255|HAMAP-Rule:MF_00847}.
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};
CC -!- SUBUNIT: Monomer. Probably contacts ribosomal proteins L1, L5, L33 and
CC S7, the 16S and 23S rRNA and the P-site containing tRNA(fMet).
CC {ECO:0000255|HAMAP-Rule:MF_00847}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00847}.
CC Note=Associates with ribosomes and polysomes. {ECO:0000255|HAMAP-
CC Rule:MF_00847}.
CC -!- DOMAIN: The arm domain is inserted in the first ABC transporter domain.
CC Probably contacts ribosomal protein L1. {ECO:0000255|HAMAP-
CC Rule:MF_00847}.
CC -!- DOMAIN: The P-site tRNA interaction motif (PtIM domain) probably
CC interacts with the P-site tRNA(fMet) as well as the 23S rRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00847}.
CC -!- DISRUPTION PHENOTYPE: No visible growth or ribosome-associated
CC phenotype. {ECO:0000269|PubMed:30597160}.
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}.
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DR EMBL; AE014075; AAN83898.1; -; Genomic_DNA.
DR RefSeq; WP_000046754.1; NC_004431.1.
DR AlphaFoldDB; A0A0H2VFI8; -.
DR SMR; A0A0H2VFI8; -.
DR STRING; 199310.c5478; -.
DR EnsemblBacteria; AAN83898; AAN83898; c5478.
DR KEGG; ecc:c5478; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OMA; ISYKPQY; -.
DR Proteomes; UP000001410; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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 ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Protein biosynthesis; Repeat; RNA-binding; rRNA-binding;
KW Translation regulation; tRNA-binding.
FT CHAIN 1..555
FT /note="Energy-dependent translational throttle protein
FT EttA"
FT /id="PRO_0000449037"
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 REGION 242..322
FT /note="PtIM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
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: Causes growth defect at 18 degrees Celsius in
FT bipA deletion strain; when associated with Q-456 (called
FT EQ2)."
FT /evidence="ECO:0000269|PubMed:30597160"
FT MUTAGEN 470
FT /note="E->Q: Causes growth defect at 18 degrees Celsius in
FT bipA deletion strain; when associated with Q-188 (EQ2)."
FT /evidence="ECO:0000269|PubMed:30597160"
SQ SEQUENCE 555 AA; 62415 MW; 94B41B47CCF3A6C1 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 SLSFSIPKGA IVGIIGPNGA
GKSTLFRMIS GQEQPDSGTI TLGETVKLAS VDQFRDSMDN SKTVWEEVSG GLDIMKIGNT
EMPSRAYVGR FNFKGVDQGK RVGELSGGER GRLHLAKLLQ VGGNMLLLDE PTNDLDIETL
RALENALLEF PGCAMVISHD RWFLDRIATH ILDYQDEGKV EFFEGNFTEY EEYKKRTLGA
DALEPKRIKY KRIAK
