ID   EF2_SULIA               Reviewed;         736 AA.
AC   C3N5S0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=M1627_1463;
OS   Sulfolobus islandicus (strain M.16.27).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.27;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001401; ACP55345.1; -; Genomic_DNA.
DR   RefSeq; WP_012711411.1; NC_012632.1.
DR   AlphaFoldDB; C3N5S0; -.
DR   SMR; C3N5S0; -.
DR   EnsemblBacteria; ACP55345; ACP55345; M1627_1463.
DR   GeneID; 7814307; -.
DR   GeneID; 7939926; -.
DR   GeneID; 8761446; -.
DR   KEGG; sim:M1627_1463; -.
DR   HOGENOM; CLU_002794_11_1_2; -.
DR   OMA; GVMTQTE; -.
DR   Proteomes; UP000002307; 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.
FT   CHAIN           1..736
FT                   /note="Elongation factor 2"
FT                   /id="PRO_1000202313"
FT   DOMAIN          18..234
FT                   /note="tr-type G"
FT   BINDING         27..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         93..97
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         147..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   MOD_RES         603
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   736 AA;  81793 MW;  90AE4BBCFF214B8A CRC64;
     MPRYKTVEQV LSLMKDRTRV RNIGIIAHVD HGKTTTSDTL LAASGIISPK VAGEALALDY
     LSVEQQRGIT VKAANISLYH EAEGKGYVIN LIDTPGHVDF SGRVTRSLRV LDGSIVVVDA
     VEGIMTQTET VLRQSLEERV RPILFINKVD RLVKELKLSP QEMLNRLLDI IRQVNNLIDM
     YGEPEFKEKW MINPQAGNVI FGSAKDKWGF SLPMAQKKGI NMKNVIDAYT ASDKSKLEEL
     AAQAPINEAL LDAAIKFVPN PIEAQKYRIP KIWKGDLDNE LAKAMLNADP NGPIVFMITD
     MKVDPHAGLV ATGRVFSGTL RSGEELWLVN AKTSQRILQV SLYMGPTREL AEEIPAGNIA
     AVLGLDRARS GETAISVGFS NVQGSFERLH YISEPVVTIA VEPKNPKDLT KMIDALRKLS
     IEDPNLVVKI NEETGEYLLS GMGFLHLEVS LQLLRENYGI DVVTTPPIVV YRESIRAKSQ
     VFEGKSPNKH NKFYLSVEPL NDKTIELISN GTIREDMDSK EMAKILRDEA SWDYDEAKRI
     IAIDENVNVF VDLTSGVQHL REVMDTVLQG FRLAMKEGPL AHEPIRGVKV ILHDAVIHED
     PAHRGPAQIY PAVRNSIFAG FLTSRPTLLE PIQKLDIRVP ADLIGNVTAV ITRKRGKILD
     VSQIANMSRI TAEIPVSESY DMASELRGST GGRAFWGTEF SRWAPVPDSI LLDVVTKIRE
     RKGLPKELPK VEDFLS