ID J7F5U8_SACJA Unreviewed; 410 AA.
AC J7F5U8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Elongation factor Tu, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN Name=tufA {ECO:0000256|HAMAP-Rule:MF_00118,
GN ECO:0000313|EMBL:AFC40171.1};
GN ORFNames=LJCPDNA_108 {ECO:0000313|EMBL:AFC40171.1};
OS Saccharina japonica (Sweet kelp) (Laminaria japonica).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AFC40171.1}.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Laminariales; Laminariaceae; Saccharina.
OX NCBI_TaxID=88149 {ECO:0000313|EMBL:AFC40171.1};
RN [1] {ECO:0000313|EMBL:AFC40171.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23305622; DOI=10.1016/j.margen.2012.12.002;
RA Wang X., Shao Z., Fu W., Yao J., Hu Q., Duan D.;
RT "Chloroplast genome of one brown seaweed, Saccharina japonica
RT (Laminariales, Phaeophyta): its structural features and phylogenetic
RT analyses with other photosynthetic plastids.";
RL Mar. Genomics 10:1-9(2013).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00003982, ECO:0000256|HAMAP-Rule:MF_00118,
CC ECO:0000256|RuleBase:RU000325}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC Rule:MF_00118, ECO:0000256|RuleBase:RU000325}.
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DR EMBL; JQ405663; AFC40171.1; -; Genomic_DNA.
DR RefSeq; YP_006639117.1; NC_018523.1.
DR AlphaFoldDB; J7F5U8; -.
DR GeneID; 13530512; -.
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:UniProtKB-UniRule.
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 CDD; cd03707; EFTU_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AFC40171.1};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00118};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00118}; Plastid {ECO:0000313|EMBL:AFC40171.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00118}.
FT DOMAIN 10..215
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 410 AA; 44865 MW; C0A228145A7B4867 CRC64;
MAREKYDRTK PHINIGTIGH VDHGKTTLTA AITAVLSLTG DSTNAKKYED IDAAPEERAR
GITINTAHVE YETESRHYAH VDCPGHADYV KNMITGAAQM DGAILVVSAA DGPMPQTREH
ILLSKQVGVP HIVVFLNKED QVDDLELVEL VELEVRELLS NYDFPGDDIP ILTGSALQAL
DAINNEPTLK KGDNKWVDKI YSLMDSVDSY IPTPIRDVDK PFLMAIEDVF SITGRGTVAT
GKIDRGIVKV GETVDLVGLG DTKSTTVTGV EMFQKTLDEG VAGDNVGILL RGLQKDEIER
GMVLSKPGTI TPHNTFESEL YILTKEEGGR HTPFFPGYRP QFYVRTTDVT GEIISFITDE
GEKTLMVMPG DRVKMTAKLI SLIAIEEGMR FAIREGGRTI GAGVVSKIIQ
//
