EF2_METRM
ID EF2_METRM Reviewed; 731 AA.
AC D3E3N9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=mru_1300;
OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS OCM 146 / M1) (Methanobacterium ruminantium).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=634498;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1;
RX PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA Janssen P.H., Dey D., Attwood G.T.;
RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT reveals new possibilities for controlling ruminant methane emissions.";
RL PLoS ONE 5:E8926-E8926(2010).
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; CP001719; ADC47150.1; -; Genomic_DNA.
DR RefSeq; WP_012956099.1; NC_013790.1.
DR AlphaFoldDB; D3E3N9; -.
DR SMR; D3E3N9; -.
DR STRING; 634498.mru_1300; -.
DR EnsemblBacteria; ADC47150; ADC47150; mru_1300.
DR GeneID; 8770951; -.
DR KEGG; mru:mru_1300; -.
DR PATRIC; fig|634498.28.peg.1303; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; QFAEMYT; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000008680; 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 CDD; cd03713; EFG_mtEFG_C; 1.
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; IPR035649; EFG_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..731
FT /note="Elongation factor 2"
FT /id="PRO_0000408961"
FT DOMAIN 19..234
FT /note="tr-type G"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 94..98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT MOD_RES 598
FT /note="Diphthamide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 731 AA; 80730 MW; B39176940F169A92 CRC64;
MSRRDKMIAK IKELMYKPEY IRNIGICAHI DHGKTTLSDN LLAGAGLISE DLAGEALGMD
TKKDEQERGI TIDAANASMV QEYEGEQYLI NLIDTPGHVD FGGDVTRAMR AVDGAVVVVC
AVDGVMPQTE TVLKQALREN VKPVLFINKV DRLINELKLG PEELLKQLTS IIVEVNALIK
SLAPKDKKNE WMVNVEEGSV AFGSAFKNWA INIPKMQETK FTFKDIIDYC NEGKEDELKQ
LLPLTEVLLN MVVKHLPSPN VAQVYRVPKI WDGDIESEVG QTMIKMSPDG PLAGMITNVA
VDKHAGIVAT CRIYGGTLEK SSEIYLVGSH GKARVQQAGI FMGAETIDTG KVPVGNIAYL
TGVKGASAGE TICSADCIID EFEPIDHISE PVVTVAVEAK NTKDLPKLIE VLRQVSKEDP
TIKVEINETT GEQLISGMGE LHLEVVTNRI INDKKLEILV SEPIIVYKES VLGHSPVIEG
KSPNKHNRFY IDVQPLDKPL YDALIEGDLK EGRIKTKETA QDFIELGMDK EEARRVWDVY
NRSMFINMTR GIQYLDEVKE LLLEGFEAAL KDGPLANEEA VGLKFILSDA KLHEDAVHRG
PAQVLPAIKK AIYASIMSAN PCLLEPIQKV FISAPLEYMG NCNKDIQNRR GRIIGQETKG
VIAEMDFEVP IAKMFGFAGD IRSATGGKGD FSTEMKGFET LPIYLQDDIV RQIRTRKGLS
PEPYGPEHYS A
