EF2_METTH
ID EF2_METTH Reviewed; 730 AA.
AC O27131;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=MTH_1057;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85548.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85548.1; ALT_INIT; Genomic_DNA.
DR PIR; E69007; E69007.
DR RefSeq; WP_048060960.1; NC_000916.1.
DR AlphaFoldDB; O27131; -.
DR SMR; O27131; -.
DR STRING; 187420.MTH_1057; -.
DR PRIDE; O27131; -.
DR EnsemblBacteria; AAB85548; AAB85548; MTH_1057.
DR GeneID; 1471465; -.
DR KEGG; mth:MTH_1057; -.
DR PATRIC; fig|187420.15.peg.1036; -.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR Proteomes; UP000005223; 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..730
FT /note="Elongation factor 2"
FT /id="PRO_0000091037"
FT DOMAIN 19..260
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 597
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 730 AA; 80924 MW; 07549350848DE81C CRC64;
MSRRAKMISK IKELMYQPEY IRNIGIVAHI DHGKTTLSDN LLAGAGMISA ELAGDQRFLD
FDEQEQARGI TIDAANVSMV HSYEGNEYLI NLIDTPGHVD FGGDVTRAMR AVDGAVVVVC
AVEGIMPQTE TVLRQALKEN VRPVLFINKV DRLINELKLD ASELQERFVK IIANANKLIK
NMAPEEFRDK WQVRVEDGSV AFGSAYHNWA INVPIMQETG INFNDIYKYC TEDNQKELAQ
KVPLHQVLLG MVVEHLPSPA ESQAYRVPII WSGDLESEEG QAMLKTDPEG PLAVMVTDVS
IDKHAGEVAT GRVYGGAIEK GSEVFLVGSH SKARVQQVGV YMGPERVNTD KVPAGNIVAI
TGAKNAVAGE TICDTGRKIK AFEGLEHISE PVVTVAVEAK NTKDLPKLIE VLRQVGKEDP
TVRVEINEET GEHLISGMGE LHLEIIAYRI NEKGVEIETS EPIVVYRETV AGTAGPVEGK
SPNKHNRFYI EIEPVEASVM QAIQEGKIKE GRVKGKEMAK NFIEAGMDKE EARRVWDVYE
KNLFINMTRG IQYLDEIKEL LMDGFESAMD NGPVAKEKVM GVKIKLMDAK IHEDAVHRGP
AQVLPAIRKG IFGAMMSAEP VLLEPIQKVF INVPQDYMGS ATREIQNRRG QIVNMTQEGD
MVTVESTVPV AEMFGFAGDI RSATEGRCLW STENAGFERL PNELQHTITR EVRTRKGLSP
EPYRADHYLG
