ID B3DR17_BIFLD Unreviewed; 559 AA.
AC B3DR17;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=uup3 {ECO:0000313|EMBL:ACD99300.1};
GN Synonyms=ettA {ECO:0000256|HAMAP-Rule:MF_00847};
GN OrderedLocusNames=BLD_1855 {ECO:0000313|EMBL:ACD99300.1};
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD99300.1, ECO:0000313|Proteomes:UP000002419};
RN [1] {ECO:0000313|EMBL:ACD99300.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD99300.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA Lee J.H., O'Sullivan D.J.;
RT "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT DJO10A and construction of a shuttle cloning vector.";
RL Appl. Environ. Microbiol. 72:527-535(2006).
RN [2] {ECO:0000313|EMBL:ACD99300.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD99300.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00847}.
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DR EMBL; CP000605; ACD99300.1; -; Genomic_DNA.
DR RefSeq; WP_012472193.1; NZ_AABM02000014.1.
DR AlphaFoldDB; B3DR17; -.
DR KEGG; blj:BLD_1855; -.
DR HOGENOM; CLU_000604_36_0_11; -.
DR Proteomes; UP000002419; 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; 2.
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 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..258
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 324..541
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 94..138
FT /note="Arm"
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 559 AA; 62029 MW; 05A52595A1436BEF CRC64;
MAEFVFQMIK ARKSYGDRVI LDDVTLSFLP GAKIGVVGPN GMGKSTLLKI MAGLETVSNG
EAALTPGFTV GILQQEPPLD DTKTVGENIK MAFGPIAEKV ARFNEIGEEM ANPDADFDAL
MEEMGKLQTE IDAADGWDLD SQLEQAMDAL QCPDPDTPVN VCSGGERRRV ALCKLLLEAP
DLLLLDEPTN HLDAESILWL EQFLHQYKGA VIAVTHDRYF MDNVAEWICE VDRGHLYPYK
GNYSTYLETK AKRLEIQGAK DAKLAKRLKN ELDWVRSSPK ARQAKNKARL ERYDQMENEA
RNNKKLDFSE IQIPAGPRLG STVLEANHIH KAFGERVLID DLSFTLPRNG IVGVIGPNGV
GKSTLFKTIV GLEPLTSGEL KIGDTVKISY VDQNREGLDP NKNLWEAVSD GLDFIEVAGV
EVPTRAYVAS FGFKGADQQK LTGVLSGGER NRLNLALTLK QGGNLLLLDE PTNDLDVETL
ESLENALLEF PGCAVVISHD RWFLDRVATH ILAWEGDDDN PAKWYWFEGN FQAYQENKVA
RLGEDAARPH RLHKKLVRG
//
