EFTUB_NICSY
ID EFTUB_NICSY Reviewed; 485 AA.
AC Q43364; Q7DNA4;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Elongation factor TuB, chloroplastic;
DE Short=EF-TuB;
DE Flags: Precursor;
GN Name=TUFB;
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8087886; DOI=10.1007/bf00309543;
RA Sugita M., Murayama Y., Sugiura M.;
RT "Structure and differential expression of two distinct genes encoding the
RT chloroplast elongation factor Tu in tobacco.";
RL Curr. Genet. 25:164-168(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-485.
RC TISSUE=Leaf;
RX PubMed=8358028; DOI=10.1007/bf00027363;
RA Murayama Y., Matsubayashi T., Sugita M., Sugiura M.;
RT "Purification of chloroplast elongation factor Tu and cDNA analysis in
RT tobacco: the existence of two chloroplast elongation factor Tu species.";
RL Plant Mol. Biol. 22:767-774(1993).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
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; D11470; BAA02028.1; -; Genomic_DNA.
DR EMBL; D11376; BAA01975.1; -; mRNA.
DR PIR; S36184; S36184.
DR RefSeq; XP_009772722.1; XM_009774420.1.
DR AlphaFoldDB; Q43364; -.
DR SMR; Q43364; -.
DR STRING; 4096.XP_009772722.1; -.
DR PRIDE; Q43364; -.
DR GeneID; 104223071; -.
DR KEGG; nsy:104223071; -.
DR eggNOG; KOG0460; Eukaryota.
DR Proteomes; UP000189701; Unplaced.
DR GO; GO:0009507; C:chloroplast; 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; 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 2: Evidence at transcript level;
KW Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 77..485
FT /note="Elongation factor TuB, chloroplastic"
FT /id="PRO_0000007456"
FT DOMAIN 86..290
FT /note="tr-type G"
FT REGION 95..102
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 136..140
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 157..160
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 212..215
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 250..252
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 95..102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 157..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 485 AA; 52688 MW; FE88EF5D48B92D29 CRC64;
MASISAASAT ATASTKLAYP YSPSSSSSSS NTAAVFPSNS SKLILSSSFT PTPSTLFLHS
PTTTPSTTHP RRFTVRAARG KFERKKPHVN IGTIGHVDHG KTTLTAALTM ALASMGNSAP
KKYDEIDAAP EERARGITIN TATVEYETEN RHYAHVDCPG HADYVKNMIT GAAQMDGAIL
VVSGADGPMP QTKEHILLAK QVGVPNMVVF LNKQDQVDDE ELLELVELEV RELLSSYEFP
GDEIPIISGS ALLALEALMA NPSIKRGENQ WVDKIYQLMD NVDEYIPIPQ RQTELPFLMA
IEDVFSITGR GTVATGRVER GTVKVGEIVD IVGLKDTRNT TVTGVEMFQK ILDEAMAGDN
VGLLLRGIQK IDIQRGMVLA KPGTITPHTK FEALVYVLKK EEGGRHSPFF AGYRPQFYMR
TTDVTGKVTV IMSDKGEESK MVMPGDRVNM VVELIMPVAC EQGMRFAIRE GGKTVGAGVI
QKILE