ID A0A6S6M2D3_9DELT Unreviewed; 561 AA. AC A0A6S6M2D3; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 10-FEB-2021, entry version 2. 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 ORFNames=GEOBRER4_32970 {ECO:0000313|EMBL:BCG48547.1}; OS Geobacter bremensis. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=60035 {ECO:0000313|EMBL:BCG48547.1, ECO:0000313|Proteomes:UP000515472}; RN [1] {ECO:0000313|EMBL:BCG48547.1, ECO:0000313|Proteomes:UP000515472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R4 {ECO:0000313|EMBL:BCG48547.1, RC ECO:0000313|Proteomes:UP000515472}; RA Meng L., Yoshida N.; RT "Interaction of electrochemicaly active bacteria, Geobacter bremensis R4 on RT different carbon anode."; RL Submitted (JUN-2020) 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}. 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; AP023213; BCG48547.1; -; Genomic_DNA. DR Proteomes; UP000515472; Chromosome. DR HAMAP; MF_00847; EttA; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032781; ABC_tran_Xtn. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00847, ECO:0000256|PROSITE-ProRule:PRU00434}; KW 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, ECO:0000256|PROSITE-ProRule:PRU00434}; KW 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 10..264 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT DOMAIN 329..555 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT NP_BIND 42..49 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" FT NP_BIND 361..368 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" FT NP_BIND 361..368 FT /note="ATP 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847" FT REGION 247..327 FT /note="PtIM" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847" SQ SEQUENCE 561 AA; 63164 MW; 3454E9762E3EBB83 CRC64; MALDPNKVIY SMIGVSKFYD KKPVLKDIYL SYFYGAKIGV LGLNGSGKSS LLKILAGVDK EFNGKTILSP GYTVGYLAQE PQLDPNKTVR QCVEEGVQEI VDLMNEFNEI NMKFGEEMSD ADMEKLCDRQ AKVQEKLDHF DAWDLDSRLE LAMDALRCPP PETNVANLSG GEKRRVALCR LLLQKPDILL LDEPTNHLDA ESVAWLEQHL QRYAGTIIAV THDRYFLDNV AGWILELDRG QGIPWQGNYS SWLEQKEKRL AQEEKTESER QKTLKRELEW IRMSPKGRHA KGKARINSYE DLLNTESEKR GRDLEIYIPP GPRLGGVVVE AENVAKGYGD KLLVEGMEFR LPPGGIVGVI GPNGAGKTTL FRMITGEEKP DSGTFKIGET VKLAYVDQSR DALDPEQTIW EAISGGQEQL QLGKQLVNSR AYVARFNFSG ADQQKKLGML SGGERNRVHL AKMLKEGGNV ILLDEPTNDL DVNTMRALEE ALENFAGCAV VISHDRWFLD RIATHILAFE GDSKVVWFEG NYSEYEEDRH ARLGTAADQP HRIMYRQLTR V //