ID   EFGC_ARAHY              Reviewed;         109 AA.
AC   P86349;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Elongation factor G, chloroplastic {ECO:0000250|UniProtKB:P34811};
DE            Short=cEF-G;
DE   Flags: Fragments;
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=cv. Vemana; TISSUE=Leaf;
RX   PubMed=20345176; DOI=10.1021/pr901009n;
RA   Katam R., Basha S.M., Suravajhala P., Pechan T.;
RT   "Analysis of peanut leaf proteome.";
RL   J. Proteome Res. 9:2236-2254(2010).
CC   -!- FUNCTION: Chloroplast-localized elongation factor EF-G involved in
CC       protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal
CC       translocation step during translation elongation. During this step, the
CC       ribosome changes from the pre-translocational (PRE) to the post-
CC       translocational (POST) state as the newly formed A-site-bound peptidyl-
CC       tRNA and P-site-bound deacylated tRNA move to the P and E sites,
CC       respectively. Catalyzes the coordinated movement of the two tRNA
CC       molecules, the mRNA and conformational changes in the ribosome (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:P34811}.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC       G/EF-2 subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86349; -.
DR   UniPathway; UPA00345; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   SUPFAM; SSF54211; SSF54211; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Plastid; Protein biosynthesis.
FT   CHAIN           <1..>109
FT                   /note="Elongation factor G, chloroplastic"
FT                   /id="PRO_0000405238"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000305"
FT   NON_CONS        35..36
FT                   /evidence="ECO:0000305"
FT   NON_CONS        47..48
FT                   /evidence="ECO:0000305"
FT   NON_CONS        60..61
FT                   /evidence="ECO:0000305"
FT   NON_CONS        87..88
FT                   /evidence="ECO:0000305"
FT   NON_CONS        94..95
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         109
SQ   SEQUENCE   109 AA;  11954 MW;  D829343249433BA9 CRC64;
     NFSVFAMSAD GDAKILYYTG RNKAIVWSGE ELGAKLAQED PSFHFSRVEA NVGAPQVNYR
     QSGGQGQFAD ITVRFEPMDP GSGYEFKMLE PIMKRGQINS FGDKPGGLK