EFTU_DELAC
ID EFTU_DELAC Reviewed; 23 AA.
AC P83710;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 11-DEC-2019, entry version 29.
DE RecName: Full=Elongation factor Tu;
DE Short=EF-Tu;
DE Flags: Fragments;
GN Name=tuf;
OS Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=80866;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=MC1;
RX PubMed=15073309; DOI=10.1099/mic.0.26774-0;
RA Benndorf D., Davidson I., Babel W.;
RT "Regulation of catabolic enzymes during long-term exposure of Delftia
RT acidovorans MC1 to chlorophenoxy herbicides.";
RL Microbiology 150:1005-1014(2004).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: The C-terminus may be subjected to proteolysis.
CC -!- MISCELLANEOUS: Different sizes are detectable in 2D-gels depending on
CC concentration of the herbicide dichlorprop [(R)-2-(2,4-
CC dichlorophenoxy)propionate].
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC Tu/EF-1A subfamily. {ECO:0000305}.
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DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN <1..>23
FT /note="Elongation factor Tu"
FT /id="PRO_0000091315"
FT NON_CONS 15..16
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 23
SQ SEQUENCE 23 AA; 2304 MW; 330DE85D380CE1CC CRC64;
NMITGAAQMX GAILVAYDSI XAA