ID   EFGC_PEA                Reviewed;         141 AA.
AC   P35450;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Elongation factor G, chloroplastic;
DE            Short=cEF-G;
DE            Short=chlEF-G;
DE   Flags: Fragment;
GN   Name=fusA;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-15.
RX   PubMed=8311443; DOI=10.1006/abbi.1994.1016;
RA   Akkaya M.S., Welcsh P.L., Wolfe M.A., Duerr B.K., Becktel W.J.,
RA   Breitenberger C.A.;
RT   "Purification and N-terminal sequence analysis of pea chloroplast protein
RT   synthesis factor EF-G.";
RL   Arch. Biochem. Biophys. 308:109-117(1994).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; L16508; AAA33654.1; -; mRNA.
DR   PIR; S70781; S70781.
DR   AlphaFoldDB; P35450; -.
DR   SMR; P35450; -.
DR   PRIDE; P35450; -.
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:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 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..>141
FT                   /note="Elongation factor G, chloroplastic"
FT                   /id="PRO_0000091279"
FT   DOMAIN          12..>141
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         21..28
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   NON_TER         141
SQ   SEQUENCE   141 AA;  15977 MW;  BF6C7FC1B829A8FD CRC64;
     ATEDGKRAVP LKDYRNIGIM AHIDAGKTTT TERILFYTGR NYKIGEVHEG TATMDWMEQE
     QERGITITSA ATTTFWDKHR INIIDTPGHV DFTLEVERAL RVLDGAICLF DSVAGVEPQS
     ETVWRQADRY GVPRICFVNK M