EF2_THEAC
ID EF2_THEAC Reviewed; 732 AA.
AC P26752;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=Ta0446;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=2044939; DOI=10.1016/0378-1097(91)90526-g;
RA Pechmann H.J.L., Tesch A., Klink F.;
RT "Cloning and sequencing of the fus-gene encoding elongation factor 2 in the
RT archaebacterium Thermoplasma acidophilum.";
RL FEMS Microbiol. Lett. 63:51-56(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; X56840; CAA40171.1; -; Genomic_DNA.
DR EMBL; AL445064; CAC11588.1; -; Genomic_DNA.
DR PIR; S36089; S36089.
DR RefSeq; WP_010900873.1; NC_002578.1.
DR AlphaFoldDB; P26752; -.
DR SMR; P26752; -.
DR STRING; 273075.Ta0446; -.
DR EnsemblBacteria; CAC11588; CAC11588; CAC11588.
DR GeneID; 1456055; -.
DR KEGG; tac:Ta0446; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000001024; 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..732
FT /note="Elongation factor 2"
FT /id="PRO_0000091050"
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: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 598
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT CONFLICT 730
FT /note="A -> D (in Ref. 1; CAA40171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 81217 MW; C69D533CC852A1F4 CRC64;
MGRKEDNIEK ALKIVEHTEL IRNIGIVAHI DHGKTTLSDN LIAGAGMMSE ELAGKQLVLD
YDEQEQARGI TINAAVASMV HTFQGKEYLI NLIDTPGHVD FGGDVTRAMR AVDGVIVVVD
SVEGVMPQTE TVIRQALREH VKPVLFINKI DRLINELRLN SDEMQKRFTK IITDVNRLIS
KYAPQQFTKE WQVSVQDGRV AFGSAYNNWA ISIPAMAETK ITFKDIVEYV KNGKQKELAQ
KNQLHKIILN MVIRHLPDPK TAQSYRIKQI WKGDLDSEIG KAMINCDYKG PVAMMVTKII
IDPHAGEIAI GRLFSGTVKK GTDLYISGAG KGKVQTLAMM VGPDRIPVDE ITAGNIAAIV
GLKGAIAGAT VSSLENMVPF EPMIHYSEPV VTLAIEAKHT ADLPRLIEVL RDISKADPSI
QVDINQETGE HLISGMGELH LDVTLYRIKN DYKVEVETSD PIVVYRETVE KKGGPFEGKS
PNKHNRFYFE VEPLKPEVIQ AIEDGDIPQG SKFKDKKALV ELLVSKGIDR DEAKGLVCVE
GTNMMFDVTR GIQYLDETME LLIEAFVEVM NRGPLANEKV FGVKARLVDA KLHEDSIHRG
PAQVIPAGRN SIYGAMCEAK RVLLEPVQRV FINVPQEEMG AAINEIQQRR GIIEDMKQEG
DEISLTAKVP VAGMFGFASA IRGATGGKVL WSFENAGYQK VPPELQDSIV RSIRERKGLR
QEPYDADYYA SM
