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Database: UniProt
Entry: C3JRQ9_RHOER
LinkDB: C3JRQ9_RHOER
Original site: C3JRQ9_RHOER 
ID   C3JRQ9_RHOER            Unreviewed;       571 AA.
AC   C3JRQ9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=RHOER0001_0003 {ECO:0000313|EMBL:EEN85712.1};
OS   Rhodococcus erythropolis SK121.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN85712.1, ECO:0000313|Proteomes:UP000005836};
RN   [1] {ECO:0000313|EMBL:EEN85712.1, ECO:0000313|Proteomes:UP000005836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK121 {ECO:0000313|EMBL:EEN85712.1,
RC   ECO:0000313|Proteomes:UP000005836};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-2009) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEN85712.1}.
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DR   EMBL; ACNO01000075; EEN85712.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3JRQ9; -.
DR   Proteomes; UP000005836; Unassembled WGS sequence.
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          18..268
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          334..551
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT   BINDING         366..373
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
SQ   SEQUENCE   571 AA;  63691 MW;  B57A9B991D8656C2 CRC64;
     MGYRTNTDRL AVMAEFIYTM KKVRKAHGDK VILDDVTMSF YPGAKIGVVG PNGAGKSSIL
     KIMAGLDQPG NGEAFLAPGA TVGILMQEPE LDETKTVREN VEDGLGETMV QLKRYNEIAE
     LMATDYSDEL MEEMGELQEK LDHADAWEID SQLEQAMDAL RCPPPEEMVT HLSGGEKRRV
     ALCKLLLSKP DLLLLDEPTN HLDAESVLWL EQHLAAYPGA ILAVTHDRYF LDHVAQWICE
     VDRGRLYPYE GNYSTYLEQK AARLEVAGKK DQKLQKRLKD ELAWVRSGAK ARQAKNKARL
     DRYEEMANEA EKTRKLDFDE IQIPAPPRLG DVVVEVSNLD KGFDGRVLIK DLSFTLPRNG
     IVGVIGPNGV GKTTLFKTIV GLEEPDAGEV KIGQTVKLSY VDQNRSGIDP KKTVWETVSD
     GLDFIVVGQT EFPSRAYISS FGFKGHDQQK PAGVLSGGER NRLNLAMTLK QGGNLILLDE
     PTNDLDVETL GSLENALEEF PGCAVVISHD RWFLDRTCTH ILAWEGGFGD NEAAWYWYEG
     NFEGYEANKV ERLGPDAARP HRVTHRKLTR D
//
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