ID Q4JWW4_CORJK Unreviewed; 556 AA.
AC Q4JWW4;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=jk0534 {ECO:0000313|EMBL:CAI36693.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36693.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI36693.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI36693.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI36693.1; -; Genomic_DNA.
DR RefSeq; WP_005296530.1; NC_007164.1.
DR AlphaFoldDB; Q4JWW4; -.
DR STRING; 306537.jk0534; -.
DR GeneID; 3432246; -.
DR KEGG; cjk:jk0534; -.
DR PATRIC; fig|306537.10.peg.546; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_11; -.
DR OrthoDB; 3239744at2; -.
DR Proteomes; UP000000545; 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 Reference proteome {ECO:0000313|Proteomes:UP000000545};
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..256
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 322..539
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT BINDING 354..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
SQ SEQUENCE 556 AA; 62551 MW; 0008DB7F35098D15 CRC64;
MGEFIYTMKN VRKAHGDKVI LDNVTMAFYP GAKIGVVGPN GAGKSSILKI MAGIDQPSNG
EAFLDPGATV GILLQEPPLN EEKTVRQNVE EGMGEIFEIR QRYEEIAEEM ATNYTDELME
EMTDLQEKID AADAWELDSK IEQAMEALRC PPSDEPVTHL SGGERRRVAL AKLLLSEPDL
LLLDEPTNHL DAESVLWLEQ HLKDYKGAVL AVTHDRYFLD HVAGWICEVD RGKLYPYEGN
YSTYLETKAK RLEVAGKKDA KLQKRLKEEL QWVRSGAKAR QAKNKARLQR YEEMAAEAEK
YKKLDFEEIQ IPTPPRLGNQ VVEVKDLNKG FDGRTLIKDL SFTLPRNGIV GVIGPNGVGK
TTLFKTIVGL EEPDSGEVKV GSTVQLSYVD QNRENIDPEQ TVWEVVSDGL DYIHVGQNEM
PSRAYLSAFG FKGPDQQKPS KVLSGGERNR LNLALTLKQG GNLILLDEPT NDLDVETLSS
LENALQQFPG CAVVISHDRW FLDRTCTHIL AWEGNVAEGQ WYWFEGNFED YEKNKVDRLG
PEAARPHRVT HRKLTR
//
