ID B2VH30_ERWT9 Unreviewed; 555 AA.
AC B2VH30;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Energy-dependent translational throttle protein EttA {ECO:0000256|HAMAP-Rule:MF_00847};
DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00847};
DE AltName: Full=Translational regulatory factor EttA {ECO:0000256|HAMAP-Rule:MF_00847};
GN Name=yjjK {ECO:0000313|EMBL:CAO95725.1};
GN Synonyms=ettA {ECO:0000256|HAMAP-Rule:MF_00847};
GN OrderedLocusNames=ETA_06790 {ECO:0000313|EMBL:CAO95725.1};
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO95725.1, ECO:0000313|Proteomes:UP000001726};
RN [1] {ECO:0000313|EMBL:CAO95725.1, ECO:0000313|Proteomes:UP000001726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC {ECO:0000313|Proteomes:UP000001726};
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00847}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00847}.
CC Note=Associates with ribosomes and polysomes. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00847}.
CC -!- DOMAIN: The arm domain is inserted in the first ABC transporter domain.
CC Probably contacts ribosomal protein L1. {ECO:0000256|HAMAP-
CC Rule:MF_00847}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC Translational throttle EttA subfamily. {ECO:0000256|ARBA:ARBA00005868,
CC ECO:0000256|HAMAP-Rule:MF_00847}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU468135; CAO95725.1; -; Genomic_DNA.
DR RefSeq; WP_012440427.1; NC_010694.1.
DR AlphaFoldDB; B2VH30; -.
DR STRING; 465817.ETA_06790; -.
DR KEGG; eta:ETA_06790; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR OrthoDB; 9762051at2; -.
DR Proteomes; UP000001726; 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 CDD; cd03221; ABCF_EF-3; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03719; ABC_ABC_ChvD; 1.
DR PANTHER; PTHR43858; ENERGY-DEPENDENT TRANSLATIONAL THROTTLE PROTEIN ETTA; 1.
DR PANTHER; PTHR43858:SF1; NON-TRANSPORTER ABC PROTEIN; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00847}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00847};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00847};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00847}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00847};
KW Reference proteome {ECO:0000313|Proteomes:UP000001726};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00847};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00847};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00847};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW Rule:MF_00847};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00847}.
FT DOMAIN 6..259
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 324..542
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 95..139
FT /note="Arm"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT REGION 242..322
FT /note="PtIM"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
SQ SEQUENCE 555 AA; 62169 MW; 3D54D2F3AC05F18F CRC64;
MAQFVYSMHR VGKVVPPKRH ILKNISLSFF PGAKIGVLGL NGAGKSTLLR IMAGIDNDIE
GEARPQPGIK IGYLAQEPQL NLEHTVRESV EEAVAEVVGA LKRLDEVYAL YAAEDADFDK
LAKEQGVLEE IIQAHDGHNL NTQLERAADA LRLPDWDAKI ANLSGGERRR VALCRLLLEK
PDMLLLDEPT NHLDAESVAW LERFLHDFEG TVVAITHDRY FLDNVAGWIL ELDRGEGIPW
EGNYSSWLEQ KDARLAQEAS SEAARRKSIE KELEWVRQGA KGRQSKGKAR LARFEELNST
DYQKRNETNE LFIPPGARLG DKVLEVSNLR KSYGDRLLID DLTFSVPKGA IVGIIGPNGA
GKSTLFRMMS GQEQPDSGSI VLGDTVKLAS VDQFRDSMDN SKTVWEEVSG GQDIMRIGNT
EMPSRAYVGR FNFKGVDQGK RVGELSGGER GRLHLAKLLQ VGGNVLLLDE PTNDLDIETL
RALENALLEF PGCAMVISHD RWFLDRIATH ILDYQDEGKI EFFEGNFTEY EEYKKRTLGA
EALEPKRIKY KRMIK
//
