ETTA_ECO57
ID ETTA_ECO57 Reviewed; 555 AA.
AC P0A9W4; P37797;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=Z5993, ECs5349;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC Translational throttle EttA subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00847, ECO:0000305}.
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DR EMBL; AE005174; AAG59571.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38772.1; -; Genomic_DNA.
DR PIR; E91297; E91297.
DR PIR; G86138; G86138.
DR RefSeq; NP_313376.1; NC_002695.1.
DR RefSeq; WP_000046749.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A9W4; -.
DR SMR; P0A9W4; -.
DR STRING; 155864.EDL933_5735; -.
DR EnsemblBacteria; AAG59571; AAG59571; Z5993.
DR EnsemblBacteria; BAB38772; BAB38772; ECs_5349.
DR GeneID; 66671721; -.
DR GeneID; 913493; -.
DR KEGG; ece:Z5993; -.
DR KEGG; ecs:ECs_5349; -.
DR PATRIC; fig|386585.9.peg.5597; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OMA; ISYKPQY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding;
KW rRNA-binding; Translation regulation; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0A9W3"
FT CHAIN 2..555
FT /note="Energy-dependent translational throttle protein
FT EttA"
FT /id="PRO_0000093192"
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"
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
