ID   EF2_AERPE               Reviewed;         736 AA.
AC   Q9YC19;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=fusA; Synonyms=fus; OrderedLocusNames=APE_1432;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA80429.1; -; Genomic_DNA.
DR   PIR; G72621; G72621.
DR   AlphaFoldDB; Q9YC19; -.
DR   SMR; Q9YC19; -.
DR   STRING; 272557.APE_1432; -.
DR   EnsemblBacteria; BAA80429; BAA80429; APE_1432.
DR   KEGG; ape:APE_1432; -.
DR   PATRIC; fig|272557.25.peg.967; -.
DR   eggNOG; arCOG01559; Archaea.
DR   OMA; GVMTQTE; -.
DR   Proteomes; UP000002518; Chromosome.
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; Reference proteome.
FT   CHAIN           1..736
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091025"
FT   DOMAIN          19..262
FT                   /note="tr-type G"
FT   BINDING         28..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         148..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         602
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   736 AA;  81960 MW;  43981490CB5E8D64 CRC64;
     MGARVKVVSE IEKIMRNIDQ IRNIGIIAHV DHGKTTTSDS LLAAAGIISE RIAGEALVLD
     YLNVEKQRGI TVKSANVSLY HEYEGKPYVI NLIDTPGHVD FSGKVTRSLR VLDGAIVVVD
     AVEGVMTQTE TVIRQALEER VRPILFINKV DRLIKELKLP PEKIQQRFVE IIKEVNNLID
     LYAEPEFRKK WKLDPNAGMV AFGSAKDKWG ISVPQVKKKG ITFREIIQAY EKGKEAVAEL
     SKKMPLHETL LDMVIKFVPN PREAQRYRIP KIWKGDINSE IGQAMLNADP DGPLVFFIND
     VRIEKAGLVA TGRVFSGTLR SGEEVYLLNA GKKSRLLQVS IYMGPFREVT KEIPAGNIGA
     VMGFEDVRAG ETVVSLGYEE NAAPFESLRY VSEPVVTIAV EPVKIQDLPK MIEALRKLTI
     EDPNLVVKIN EETGEYLLSG MGPLHLEIAL TMLREKFGVE VKASPPIVVY RETVRQQSRV
     FEGKSPNKHN KLYISVEPLN EETITLIQNG AVTEDQDPKD RARILADKAG WDYNEARKIW
     AIDENINVFV DKTAGVQYLR EVKDTIIAGF RLALKEGPLA AEPVRGVKVV LHDAVIHEDP
     VHRGPGQLYP AVRNAIWAGI LDGRPTLLEP LQKLDIRAPM EYLSNITAVL TRKRGRIINV
     ETTGVMARII AAIPVAESFD LAGELRSATA GRAFWGVEFY GWAPVPDQML QDLIAKIRQR
     KGLPPSPPKI DDLIGP