EFTU_MESAU
ID EFTU_MESAU Reviewed; 174 AA.
AC P86251;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Elongation factor Tu, mitochondrial {ECO:0000250|UniProtKB:P49411};
DE Short=EF-Tu {ECO:0000250|UniProtKB:P49411};
DE Flags: Fragments;
GN Name=TUFM {ECO:0000250|UniProtKB:P49411};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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|UniProtKB:P49411}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49411}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC Tu/EF-1A subfamily. {ECO:0000255}.
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 AlphaFoldDB; P86251; -.
DR PRIDE; P86251; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; G_TR_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Elongation factor; GTP-binding; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN <1..>174
FT /note="Elongation factor Tu, mitochondrial"
FT /id="PRO_0000394413"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P49411"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49411"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT MOD_RES 161
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT NON_CONS 17..18
FT /evidence="ECO:0000305"
FT NON_CONS 26..27
FT /evidence="ECO:0000305"
FT NON_CONS 71..72
FT /evidence="ECO:0000305"
FT NON_CONS 96..97
FT /evidence="ECO:0000305"
FT NON_CONS 106..107
FT /evidence="ECO:0000305"
FT NON_CONS 120..121
FT /evidence="ECO:0000305"
FT NON_CONS 136..137
FT /evidence="ECO:0000305"
FT NON_CONS 166..167
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 174
SQ SEQUENCE 174 AA; 18836 MW; 213E3FD79039FE38 CRC64;
DKPHVNVGTI GHVDHGKILA EGGGAKKYEE IDNAPEERAR GITINAAHVE YSTAARHYAH
TDCPGHADYV KDPELGVKSV QKLLDAVDTY IPVPTRGTVV TGTLERGDEC ELLGHNKNIR
SLERAEAGDN LGALVRGLVM VKPGSIQPHQ KVEAQVYILS KEEGGRFTLR DGNK
