ID   EFTU_ARTPT              Reviewed;         410 AA.
AC   P13552;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
OS   Arthrospira platensis (Spirulina platensis).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Arthrospira.
OX   NCBI_TaxID=118562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2505055; DOI=10.1007/bf00330947;
RA   Buttarelli F.R., Calogero R.A., Tiboni O., Gualerzi C.O., Pon C.L.;
RT   "Characterization of the str operon genes from Spirulina platensis and
RT   their evolutionary relationship to those of other prokaryotes.";
RL   Mol. Gen. Genet. 217:97-104(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 383-410.
RX   PubMed=8277243; DOI=10.1099/00221287-139-11-2579;
RA   Sanangelantoni A.M., Tiboni O.;
RT   "The chromosomal location of genes for elongation factor Tu and ribosomal
RT   protein S10 in the cyanobacterium Spirulina platensis provides clues to the
RT   ancestral organization of the str and S10 operons in prokaryotes.";
RL   J. Gen. Microbiol. 139:2579-2584(1993).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
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|HAMAP-Rule:MF_00118}.
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DR   EMBL; X15646; CAA33673.1; -; Genomic_DNA.
DR   EMBL; Z21676; CAA79774.1; -; Genomic_DNA.
DR   PIR; S04391; S04391.
DR   AlphaFoldDB; P13552; -.
DR   SMR; P13552; -.
DR   PRIDE; P13552; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 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..410
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091388"
FT   DOMAIN          10..214
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   410 AA;  44758 MW;  2FA9C87D6DF0FB0B CRC64;
     MARAKFERNK PHVNIGTIGH VDHGKTTLTA AITMTLAASG GAKARKYDDI DAAPEEKQRG
     ITINTAHVEY ETEQRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLAKQVGVPS IVVFLNKADM VDDEELLELV ELEVRELLSS YDFPGDDIPI VSGSALKALD
     FLTENPKTTR GENDWVDKIH ALMDEVDAYI PTPERDIDKG LLDGLWEDVF SITGRGTVST
     AGIERGKVKV GDTVELIGIK DTRTTTVTGA EMFQKTLEEG MAGDNVGLLL RGIQKNDVQR
     GMVIAKPKSI TPHTKFEAEV YILKKEEGGR HTPFFKGYRP QFYVRTTDVT GTIDEFTADD
     GSTPEMVIPG DRINMTVQLI CPIAIEQGMR FAIREGGRTV GAGVVAKILA