ID   ETTA_HAEIN              Reviewed;         556 AA.
AC   P45127;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
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}; OrderedLocusNames=HI_1252;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
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; L42023; AAC22902.1; -; Genomic_DNA.
DR   PIR; G64169; G64169.
DR   RefSeq; NP_439408.1; NC_000907.1.
DR   RefSeq; WP_005650218.1; NC_000907.1.
DR   AlphaFoldDB; P45127; -.
DR   SMR; P45127; -.
DR   STRING; 71421.HI_1252; -.
DR   PRIDE; P45127; -.
DR   EnsemblBacteria; AAC22902; AAC22902; HI_1252.
DR   KEGG; hin:HI_1252; -.
DR   PATRIC; fig|71421.8.peg.1304; -.
DR   eggNOG; COG0488; Bacteria.
DR   HOGENOM; CLU_000604_36_0_6; -.
DR   OMA; ISYKPQY; -.
DR   PhylomeDB; P45127; -.
DR   BioCyc; HINF71421:G1GJ1-1283-MON; -.
DR   Proteomes; UP000000579; 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; Reference proteome; Repeat; RNA-binding;
KW   rRNA-binding; Translation regulation; tRNA-binding.
FT   CHAIN           1..556
FT                   /note="Energy-dependent translational throttle protein
FT                   EttA"
FT                   /id="PRO_0000093194"
FT   DOMAIN          7..260
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT   DOMAIN          325..551
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT   REGION          96..140
FT                   /note="Arm"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT   REGION          243..323
FT                   /note="PtIM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT   BINDING         357..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
SQ   SEQUENCE   556 AA;  62565 MW;  FCCE80E23457A493 CRC64;
     MSSQFVYTMH RVGKVVPPKR HILKDISLSF FPGAKIGVLG LNGAGKSTLL RIMAGVDKEF
     EGEARPQPGI KIGYLPQEPK LEPQQTVREA VEEAVSEVKN ALTRLDEVYA LYADPDADFD
     KLAAEQANLE AIIQAHDGHN LDNQLERAAD ALRLPDWDAK IEHLSGGERR RVALCRLLLE
     KPDMLLLDEP TNHLDAESVA WLERFLHDYE GTVVAITHDR YFLDNVAGWI LELDRGEGIP
     WEGNYSSWLE QKEKRLEQEQ ATENARQKSI AKELEWVRQN PKGRQAKSKA RMARFDELNS
     GEYQKRNETN ELFIPPGPRL GDKVIEVQNL TKSYGDRTLI DDLSFSIPKG AIVGIIGANG
     AGKSTLFRML SGQEQPDSGS VTMGETVVLA SVDQFRDSMD DKKTVWEEVS NGQDILTIGN
     FEIPSRAYVG RFNFKGVDQQ KRVGELSGGE RGRLHLAKLL QRGGNVLLLD EPTNDLDVET
     LRALENAILE FPGCAMVISH DRWFLDRIAT HILDYGDEGK VTFYEGNFSD YEEWKKKTLG
     DAATQPHRIK YKRIAK