EF2_SULTO
ID EF2_SULTO Reviewed; 737 AA.
AC Q975H5; F9VMY5;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; OrderedLocusNames=STK_04370;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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; BA000023; BAK54282.1; -; Genomic_DNA.
DR RefSeq; WP_052846316.1; NC_003106.2.
DR AlphaFoldDB; Q975H5; -.
DR SMR; Q975H5; -.
DR STRING; 273063.STK_04370; -.
DR EnsemblBacteria; BAK54282; BAK54282; STK_04370.
DR GeneID; 1458373; -.
DR KEGG; sto:STK_04370; -.
DR PATRIC; fig|273063.9.peg.507; -.
DR eggNOG; arCOG01559; Archaea.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000001015; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..737
FT /note="Elongation factor 2"
FT /id="PRO_0000091049"
FT DOMAIN 18..262
FT /note="tr-type G"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 93..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 604
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 737 AA; 81909 MW; 1551BDCFCE86A380 CRC64;
MPRYKTVEQV LSLMKDITRV RNIGIIAHVD HGKTTTSDTL LAAAGIISQK VAGEALALDY
LSVEQQRGIT VKAANISLYH EIEGKGYVIN LIDTPGHVDF SGRVTRSLRI LDGSIVVVDA
VEGIMTQTET VLRQSLEERV RPILFINKVD RLVKELKLSP QEIQKKLIDM IVEINNLIEM
YAEPEYKDAW KIKPELGNVV FGSAKDKWGF SVPIAQKKGV KFSDVVNAYS SGDKSKVEEL
ANRVPIHEAL LETVIKFVPN PRDAQKYRIP KIWKGDLDSD IAKAMINADP NGPIVLMISD
MKVDPHAGLV ATGRVFSGTL RAGEEIWLVN AKRQQRVLQV SLYMGPTREL AEEIPAGNIA
AALGLDQARS GETAVDIKYK DANVGSFESL HYVSEPVVTI SVEPKNPKDL NKMIDALRKL
SIEDPNLLVK INEETGEYLL SGMGFLHLEV SLQLLKENYG VDVVTSPPIV VYRESIRTKS
QVFEGKSPNK HNKLYISVEP LNEQTIELIA NGTIKEDMDS KEMARILKEQ ADWDYDEAKK
IVAIDENINV FVNATSGVQH LREVMDTILQ GFRLAMKEGP LAHEPIRGLK VVLHDAIIHE
DPAHRGPAQL YPAVRNAIFA GFLTSKPTLL EPLQKLDIRV PMDFVGNVSG VITRKRGKIL
NMTQMGSIAR ITAEIPVSES FELASELRAA SAGRAFWGTE FSRWAPVPDS LLLDVIMKIR
ERKGLPKELP KVEDFLA
