ID   EFG2_SYNY3              Reviewed;         691 AA.
AC   P74228;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Elongation factor G 2;
DE            Short=EF-G 2;
GN   Name=fusB; Synonyms=fus; OrderedLocusNames=sll1098;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome changes
CC       from the pre-translocational (PRE) to the post-translocational (POST)
CC       state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC       deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC       coordinated movement of the two tRNA molecules, the mRNA and
CC       conformational changes in the ribosome (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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:0000305}.
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DR   EMBL; BA000022; BAA18322.1; -; Genomic_DNA.
DR   PIR; S75863; S75863.
DR   AlphaFoldDB; P74228; -.
DR   SMR; P74228; -.
DR   IntAct; P74228; 4.
DR   STRING; 1148.1653408; -.
DR   PaxDb; P74228; -.
DR   EnsemblBacteria; BAA18322; BAA18322; BAA18322.
DR   KEGG; syn:sll1098; -.
DR   eggNOG; COG0480; Bacteria.
DR   InParanoid; P74228; -.
DR   OMA; AATTCHW; -.
DR   PhylomeDB; P74228; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00484; EF-G; 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   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..691
FT                   /note="Elongation factor G 2"
FT                   /id="PRO_0000091244"
FT   DOMAIN          8..282
FT                   /note="tr-type G"
FT   BINDING         17..24
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         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   691 AA;  75431 MW;  97F5FFAE6B99C91E CRC64;
     MARTVPLERI RNIGIAAHID AGKTTTTERI LFYSGVVHKI GEVHEGTAVT DWMAQERERG
     ITITAAAIST DWLGHHINII DTPGHVDFTI EVERSMRVLD GVIAVFCSVG GVQPQSETVW
     RQAERYQVPR IAFVNKMDRT GANFFRVCQQ IGDRLRANAV PVQIPIGSEA EFEGIVDLVR
     MKAYLYKNDL GTDIQEVPIP DSVKDKTEEY RLRLVESVAE ADDALMEKYL EGEELTADEL
     VAGLRRGTIA GTMVPVLCGS AFKNKGVQLL LDAVVDYLPS PLEVPAIEGH LPDGEVATRP
     AEDKAPLSAL AFKVMADPFG RLTFVRVYSG VLEKGSYVLN STKEKKERIS RLIILKADDR
     IEVDQLNAGD LGAVLGLKDT LTGDTLCDDQ EPIILESLFV PQPVISVAVE PKTKQDMDKL
     SKALQSLSEE DPTFRVSVDP ETNQTVIAGM GELHLEILVD RMLREFKVEA NVGAPQVAYR
     ETIRKAVQAE GKFIRQSGGK GQYGHVVIEV EPTEPGTGFE FVSKIVGGVI PKEYIAPSEQ
     GMKEACASGV LAGYPVIDLK ATLVDGSFHD VDSSEMAFKI AGSMAIREAV GQADPVLLEP
     VMKVEIEVPD DFMGNVIGDL NARRGHIEGQ ETEQGIAKVA ASVPLAEMFG YATDIRSKTQ
     GRGIFSMEFS HYAEVPRNVA EAIVAKSRGY A