ID   EF2_METBF               Reviewed;         730 AA.
AC   Q464Z3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Elongation factor 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=Mbar_A3686;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
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|HAMAP-Rule:MF_00054}.
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DR   EMBL; CP000099; AAZ72549.1; -; Genomic_DNA.
DR   RefSeq; WP_011308586.1; NC_007355.1.
DR   AlphaFoldDB; Q464Z3; -.
DR   SMR; Q464Z3; -.
DR   STRING; 269797.Mbar_A3686; -.
DR   PRIDE; Q464Z3; -.
DR   EnsemblBacteria; AAZ72549; AAZ72549; Mbar_A3686.
DR   GeneID; 3624630; -.
DR   KEGG; mba:Mbar_A3686; -.
DR   eggNOG; arCOG01559; Archaea.
DR   HOGENOM; CLU_002794_11_1_2; -.
DR   OMA; GVMTQTE; -.
DR   OrthoDB; 1642at2157; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_A; EF_G_EF_2_A; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/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; IPR004543; Transl_elong_EFG/EF2_arc.
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; TIGR00490; aEF-2; 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.
FT   CHAIN           1..730
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000225253"
FT   DOMAIN          19..228
FT                   /note="tr-type G"
FT   BINDING         28..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         94..98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         148..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   MOD_RES         596
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   730 AA;  80915 MW;  8603E1188AE21352 CRC64;
     MGRRKKMVER VTMLMNEPTK IRNIGIVAHI DHGKTTLSDN LLAGAGMISK ELAGRQLFMD
     SDEEEQERGI TIDSSNVSMV HNFDNEDYLI NLIDTPGHVD FGGDVTRAMR AVDGAVVVVD
     AVEGTMPQTE TVLRQALREH VRPVLFVNKV DRLINELKVD SQEMQIRLGK VIDHVNKLIK
     NMNPEKYKEG WRVDAAAGTV AFGSALYNWA ISVPMMKKTG VSFKDVYDYC KAGDMKSLAE
     KCPLHEAVLD MVIHFLPDPI EAQKDRVKVI WHGDENSEIG TSMTHANADG DLAFMVTDIS
     VDPHAGEVAT GRLFSGSFSR GMEVFTSGTA KKSRVQQVSI FMGPERLEVD KIPAGNIAAV
     TGLKEAIVGS TVTTLDGMEP FESIRHVSEP VVTVAVEAKH TKDLPKLIEV LRQVAKEDPT
     LQITLDEETG EHLMAGMGEL HLEVIAHRIE RDKNVEITTS KPIVVYRETI KKKIEPVEGK
     SPNRHNRFYI YVEPLDLEIV SAIKSGEIHM NLPELERRQK LIDLGMEKEE AKGIVGIFNS
     NIFIDMTKGI QYLNETMELI LDGFEEVMRA GPLTREPVAN VKCVLVDAKL HEDAIHRGPA
     QVIPASRQAI QAGMLMADDT LLEPYQKVFV QVPQLLMGGA TKELQGRRGI ILNMSTEGDL
     AIIEARVPVA EMFGFAGEIR SATEGRAMWS TEFGGFDIVP TSIQNDIVGQ IRERKGLKKE
     LPKASDFLSI