ID   EFTU_STIHE              Reviewed;         419 AA.
AC   Q06SH3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Stigeoclonium helveticum (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   OCC clade; Chaetophorales; Chaetophoraceae; Stigeoclonium.
OX   NCBI_TaxID=55999;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 441;
RX   PubMed=16944205; DOI=10.1007/s00438-006-0156-2;
RA   Belanger A.-S., Brouard J.-S., Charlebois P., Otis C., Lemieux C.,
RA   Turmel M.;
RT   "Distinctive architecture of the chloroplast genome in the chlorophycean
RT   green alga Stigeoclonium helveticum.";
RL   Mol. Genet. Genomics 276:464-477(2006).
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}.
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; DQ630521; ABF60202.1; -; Genomic_DNA.
DR   RefSeq; YP_764393.1; NC_008372.1.
DR   AlphaFoldDB; Q06SH3; -.
DR   SMR; Q06SH3; -.
DR   PRIDE; Q06SH3; -.
DR   GeneID; 4308433; -.
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..419
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000275381"
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:0000250"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   419 AA;  45800 MW;  1795D247B90211C8 CRC64;
     MARAKFERKK PHVNIGTIGH VDHGKTTLTA AITMALAARG GATGRKYDEI DSAPEEKARG
     ITINAAHVEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSGAD GPMPQTTEHV
     LLAKQVGVPA IVVFLNKADQ VDDPELLELV ELEVRDILDK YGFASDEVQI LSGSALLALE
     ALVENPNIKP GDSEWVDKIY NLMATVDEHI PTPKREMDKP FLLAVEDVFS ITGRGTVATG
     RVERGTLKVN ETVEIIGLRD TKTTTVTAIE MFQKTLDETI AGDNVGILLR GVQKKDIERG
     MVIAKPGTIL PHTLFEGQVY VLTAEEGGRK SGFFKGYQPQ FYVRTTDVTG KILDFSYIKQ
     RNPSELSTMH SNPMVCPGDY VNMKIQLITP IAIEKGMRFA IREGGRTVGA GMVLEILES