ID   EFTU_GUITH              Reviewed;         408 AA.
AC   P19457;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1868578; DOI=10.1007/bf00355057;
RA   Douglas S.E.;
RT   "Unusual organization of a ribosomal protein operon in the plastid genome
RT   of Cryptomonas phi: evolutionary considerations.";
RL   Curr. Genet. 19:289-294(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9137835; DOI=10.1080/15216549700202101;
RA   Wang S.L., Liu X.-Q., Douglas S.E.;
RT   "The large ribosomal protein gene cluster of a cryptomonad plastid: gene
RT   organization, sequence and evolutionary implications.";
RL   Biochem. Mol. Biol. Int. 41:1035-1044(1997).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF041468; AAC35730.1; -; Genomic_DNA.
DR   RefSeq; NP_050796.1; NC_000926.1.
DR   AlphaFoldDB; P19457; -.
DR   SMR; P19457; -.
DR   PRIDE; P19457; -.
DR   GeneID; 857104; -.
DR   HOGENOM; CLU_007265_0_0_1; -.
DR   OMA; ERPHCNV; -.
DR   GO; GO:0009507; C:chloroplast; 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   Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..408
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000091462"
FT   DOMAIN          10..213
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          59..63
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          80..83
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          135..138
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          173..175
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..84
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  44827 MW;  218420C0B1F82895 CRC64;
     MARDKFERSK PHVNIGTIGH VDHGKTTLTA AISATLSQYT GKSKKFDEID SAPEERARGI
     TINTAHVEYE TDKWYYAHVD CPGHADYVKN MITGAAQMDG AILVCSAANG PMPQTREHIL
     LAKQVGVPYI VVFLNKADMV DDEELLELVQ LEVQELLEKY DFPGSEIPFV AGSALLALEA
     VANNPTIKRG EDKWVDTIYQ LMDKVDEYIP TPERETDKAF LMAVEDVFSI TGRGTVATGR
     IERGKVKVGD TIEIVGLRET RNTTITGLEM FQKSLDEALA GDNVGILVRG IQKTDIERGM
     VLAAPGSITP HTKFEGEVYV LTKEEGGRHT PFFSGYRPQF YVRTTDVTGT IAQFTSDDGS
     TAEMVMPGDR IKMTAQLIHP IAIEKGMRFA IREGGRTVGA GVVSKIIE