ID   EFTU_MYCSY              Reviewed;          20 AA.
AC   P81407;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Elongation factor Tu;
DE            Short=EF-Tu;
DE   Flags: Fragment;
GN   Name=tuf;
OS   Mycoplasmopsis synoviae (Mycoplasma synoviae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=2109;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ULB 925 / Isolate KF9;
RX   PubMed=10220885; DOI=10.1111/j.1574-6968.1999.tb13488.x;
RA   Bencina D., Narat M., Dovc P., Drobnic-Valic M., Habe F., Kleven S.H.;
RT   "The characterization of Mycoplasma synoviae EF-Tu protein and proteins
RT   involved in hemadherence and their N-terminal amino acid sequences.";
RL   FEMS Microbiol. Lett. 173:85-94(1999).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC       Tu/EF-1A subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P81407; -.
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..>20
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091352"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2222 MW;  C3C92564B740ACC6 CRC64;
     AKLDFDRSKE HVNVGTIGVH