ID G8R3C2_OWEHD Unreviewed; 564 AA.
AC G8R3C2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-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 OrderedLocusNames=Oweho_0933 {ECO:0000313|EMBL:AEV31943.1};
OS Owenweeksia hongkongensis (strain DSM 17368 / CIP 108786 / JCM 12287 / NRRL
OS B-23963 / UST20020801).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Owenweeksiaceae;
OC Owenweeksia.
OX NCBI_TaxID=926562 {ECO:0000313|EMBL:AEV31943.1, ECO:0000313|Proteomes:UP000005631};
RN [1] {ECO:0000313|EMBL:AEV31943.1, ECO:0000313|Proteomes:UP000005631}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963
RC {ECO:0000313|Proteomes:UP000005631};
RX PubMed=23450211; DOI=10.4056/sigs.3296896;
RA Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., Del Rio T.G.,
RA Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Rohde M., Tindall B.J., Detter J.C., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Genome sequence of the orange-pigmented seawater bacterium Owenweeksia
RT hongkongensis type strain (UST20020801(T)).";
RL Stand. Genomic Sci. 7:120-130(2012).
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; CP003156; AEV31943.1; -; Genomic_DNA.
DR RefSeq; WP_014201304.1; NC_016599.1.
DR AlphaFoldDB; G8R3C2; -.
DR STRING; 926562.Oweho_0933; -.
DR KEGG; oho:Oweho_0933; -.
DR PATRIC; fig|926562.3.peg.946; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_10; -.
DR OrthoDB; 1521973at2; -.
DR Proteomes; UP000005631; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00847};
KW Reference proteome {ECO:0000313|Proteomes:UP000005631};
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 9..268
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 333..559
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 251..331
FT /note="PtIM"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT COILED 261..320
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 365..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
SQ SEQUENCE 564 AA; 63545 MW; 7017F6CCBD57B86D CRC64;
MSDDKKVIFS MSGVTKTYSS NNKTVLKNIY LSFFYGAKIG ILGLNGSGKS TLLKIIAGLE
KNYQGDVVIS PGYSVGYLSQ EPELDESKTV IDIVKEGAQE TVDILAEYNK INDDFGLPEV
YEDPDKMEKL MARQAELQDK IDATNAWELD TMLNRAMDAL RCPEPDTPIS VLSGGERRRV
ALCRLLLQQP DILLLDEPTN HLDAESVLWL EQHLQQYKGT VIAVTHDRYF LDNVAGWILE
LDRGEGIPWK GNYSSWLDQK TKRLAQEEKQ ESKRRKTLER ELDWVRMGAK GRQAKGKARL
NNYNKMLSEE QRDKEQKLEM FIPNGPRLGS NVIDANHVKK AFGEKLLYDD LNFSLPPAGI
VGIIGPNGAG KTTIFKMIMD QLEPDAGTFD VGETVKISYV DQSHEDLKPE KSIYEIISQG
NEEIEVGNQK LNARAYLSRF NFAGQDQSKK VGVLSGGERN RLHLAMALKE GGNVLLLDEP
TNDLDVNTLR ALEEALENFA GCAVIISHDR WFLDRVCTHI LAFEGDSQVY YYEGGFSDYE
ENKKKRLGDI APTRVKYKKL IKNG
//
