EFTS_ACIAD
ID EFTS_ACIAD Reviewed; 291 AA.
AC Q6FA54;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050}; OrderedLocusNames=ACIAD2268;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_00050}.
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DR EMBL; CR543861; CAG69059.1; -; Genomic_DNA.
DR RefSeq; WP_004927932.1; NC_005966.1.
DR AlphaFoldDB; Q6FA54; -.
DR SMR; Q6FA54; -.
DR STRING; 62977.ACIAD2268; -.
DR EnsemblBacteria; CAG69059; CAG69059; ACIAD2268.
DR GeneID; 45234596; -.
DR KEGG; aci:ACIAD2268; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_2_6; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR BioCyc; ASP62977:ACIAD_RS10390-MON; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 1.
DR TIGRFAMs; TIGR00116; tsf; 1.
DR PROSITE; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..291
FT /note="Elongation factor Ts"
FT /id="PRO_0000161062"
FT REGION 80..83
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 291 AA; 30882 MW; 0802D12A878296E6 CRC64;
MTAITASMVK ELRDRTGLAM MECKKALTEA NGDIELAIDN LRKSGQAKAA KKAGNIAADG
AITIVQDGNK AVLVEVNCQT DFVAKDENFS NFSNAVAKAI LASGETDAEK VAELKLEDGQ
SVEEARIALV QKIGENIQVR RAKIVEGENL AVYKHGLRIG VVVSYTGSAE TGKGIAMHVA
AFNPVAVSAE AVPADLVAKE KEIAEAKAIE SGKPANIVEK MVSGSVEKYL NEVALDRQMY
VIDNDKKVAD VLKATATNIV EFVRFEVGEG IEKKAEMSFA EEVAAAQAAA K