ID   EFTU_GLOMP              Reviewed;         235 AA.
AC   P50063;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Elongation factor Tu;
DE            Short=EF-Tu;
DE   Flags: Fragment;
GN   Name=tufA;
OS   Gloeothece membranacea (strain PCC 6501 / SAG 26.84).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Gloeothece.
OX   NCBI_TaxID=55396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7663757; DOI=10.1006/mpev.1995.1012;
RA   Delwiche C.F., Kuhsel M., Palmer J.D.;
RT   "Phylogenetic analysis of tufA sequences indicates a cyanobacterial origin
RT   of all plastids.";
RL   Mol. Phylogenet. Evol. 4:110-128(1995).
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   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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; U09434; AAC18636.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50063; -.
DR   SMR; P50063; -.
DR   GO; GO:0005737; C:cytoplasm; 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   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
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   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           <1..>235
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091329"
FT   DOMAIN          <1..125
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         47..50
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         235
SQ   SEQUENCE   235 AA;  25645 MW;  A045664B2DF04F9E CRC64;
     KNMITGAAQM DGGILVVSAA DGPMPQTREH ILLAKQVGVP SLVVFLNKED QVDDAELLEL
     VELEVRELLS IYDFPGDDIP IVIGSALKAV EALTATPTTK KGDNEWVDKI LKLMDEVDEY
     IPTPEREIDK PFLMAVEDVF SITGRGTVAT GRIERGKIKV GETVELVGIR NTRSTTVTGV
     EMFQKVLEEG MAGDNVGLLL RGIQKEDIER GMVIAKPGSI TPHTQFEGEV YVLTK