EFTS_MYCPN
ID EFTS_MYCPN Reviewed; 298 AA.
AC P78009;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Elongation factor Ts;
DE Short=EF-Ts;
GN Name=tsf; OrderedLocusNames=MPN_631; ORFNames=MP211;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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; U00089; AAB95859.1; -; Genomic_DNA.
DR PIR; S73537; S73537.
DR RefSeq; NP_110320.1; NC_000912.1.
DR RefSeq; WP_010874988.1; NC_000912.1.
DR AlphaFoldDB; P78009; -.
DR SMR; P78009; -.
DR IntAct; P78009; 1.
DR STRING; 272634.MPN_631; -.
DR EnsemblBacteria; AAB95859; AAB95859; MPN_631.
DR GeneID; 66608683; -.
DR KEGG; mpn:MPN_631; -.
DR PATRIC; fig|272634.6.peg.695; -.
DR HOGENOM; CLU_047155_0_2_14; -.
DR OMA; DAGMMDC; -.
DR BioCyc; MPNE272634:G1GJ3-1013-MON; -.
DR Proteomes; UP000000808; 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; 2.
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..298
FT /note="Elongation factor Ts"
FT /id="PRO_0000161157"
FT REGION 79..82
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 33645 MW; A44F9AC67C23FAAF CRC64;
MATKIELIKE LRKTTQASMM DCKKALEQNN DDLEKAIKWL RENGIVKSAK KLGKVAADGC
IVLHSDHHKA VMVEINSQTD FVARSQELTD FAQLMISEVF KKATPTTTIE EVTQYELQGK
EKVAERLALV ASKTDEKIVL RRLMVFESKT NHIFSYLHAN KRIGVILEVE GKFDEQDGKH
LAMHIAANSP QFIDQDNVDQ TWLANETSII KSQAKLEVQD NPKKAAFLDK TIAGRVNKLL
IDICLVNQKY LVDESKTVGQ FLKEKNSKVI HFVRFEVGEG IVKEAVDFAS EVSAQMKK