ID B1LTS1_METRJ Unreviewed; 550 AA.
AC B1LTS1;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
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=ettA {ECO:0000256|HAMAP-Rule:MF_00847};
GN OrderedLocusNames=Mrad2831_3463 {ECO:0000313|EMBL:ACB25440.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB25440.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB25440.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001001; ACB25440.1; -; Genomic_DNA.
DR RefSeq; WP_012320403.1; NC_010505.1.
DR AlphaFoldDB; B1LTS1; -.
DR STRING; 426355.Mrad2831_3463; -.
DR KEGG; mrd:Mrad2831_3463; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_5; -.
DR OrthoDB; 9762369at2; -.
DR Proteomes; UP000006589; 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 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 7..254
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 319..536
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 237..317
FT /note="PtIM"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT BINDING 351..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
SQ SEQUENCE 550 AA; 61736 MW; 6DD1BFB5EC453C6B CRC64;
MAREFIYHMR GLTKAYTGGK KVLDNVNLSF YPDAKIGVLG INGAGKSTLL KIMAGIDKEF
TGDGWVAQGA RVGYLPQEPQ LDPNKTVREN VMEGVAEKQA MLDRYNELAM NYSEETADEM
TELQDRIESL GLWELDSKVD QAMEALGCPS DEQPVATLSG GERRRIALCR LLLWEPELLL
LDEPTNHLDA ETVNWLEGHL RQYPGAILIV THDRYFLDNV TSWILELDRG KGIPYEGNYS
AWLVQKQKRL EQEGREDMAR QRSIAREQEW IAASPKARQS KSKARITRYE ELVAKQAQKV
DAAAQIVIPI DERLGNNVIE FEHLSKAFGD RLLIEDLSFK LPPGGIVGVI GPNGAGKTTL
FKMITGQEKP DSGKIEVGET VKLGYVDQSR DALDPNATVW QEVSGGNDII YFNKREINSR
AYCAAFAFKG PDQQKKVGTL SGGERNRVHL ARTLKGGANV LLLDEPTNDL DMETLRALED
ALEDYAGCAV IISHDRWFLN RIATHILAFE GDSHVEWFEG NFSDYEADKV RRLGADSIMP
KKIKYKRFSR
//
