EFTS_MYCAP
ID EFTS_MYCAP Reviewed; 298 AA.
AC A5IY49;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=MAG2600;
OS Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS agalactiae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=347257;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA Blanchard A., Citti C.;
RT "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT bacterial genome.";
RL PLoS Genet. 3:744-758(2007).
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}.
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; CU179680; CAL58958.1; -; Genomic_DNA.
DR RefSeq; WP_011949436.1; NC_009497.1.
DR AlphaFoldDB; A5IY49; -.
DR SMR; A5IY49; -.
DR STRING; 347257.MAG2600; -.
DR EnsemblBacteria; CAL58958; CAL58958; MAG2600.
DR KEGG; maa:MAG2600; -.
DR HOGENOM; CLU_047155_0_2_14; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000007065; 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; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 2.
DR TIGRFAMs; TIGR00116; tsf; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..298
FT /note="Elongation factor Ts"
FT /id="PRO_1000116763"
FT REGION 78..81
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 298 AA; 32612 MW; 875FE1613835F0E2 CRC64;
MDKMALIKEL RERTAAGMSD CKKALEVSNW DVEEAISFLK KNGKIKAASK ANRISADGLL
VEAGNNERAV LVELNCETDF VAHGEEFVAL ANTVAQTIVA NFELVKENGA EAALALKLAN
SEEILADAIS SYSAKCGEKI ELRRFVLIDA GTNQSVSTFV HINGKIGAIM LTEGSDAEAA
RNVAMHLSAM NPEYIFAEDI PGSVLEKFAS EFKEPAGFSD KPEKIQETIR KGFVDKKISE
VTLLSQKLIM DESKTVQQYL KELKLRLIKA IRFGLGEGIE KKETDFAAEV AEQMSKSM