EF2_METBU
ID EF2_METBU Reviewed; 730 AA.
AC O93632; Q12WT2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=Mbur_1171;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9845338; DOI=10.1016/s0014-5793(98)01375-1;
RA Thomas T., Cavicchioli R.;
RT "Archaeal cold-adapted proteins: structural and evolutionary analysis of
RT the elongation factor 2 proteins from psychrophilic, mesophilic and
RT thermophilic methanogens.";
RL FEBS Lett. 439:281-287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(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 (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; AF003869; AAC79155.1; -; Genomic_DNA.
DR EMBL; CP000300; ABE52094.1; -; Genomic_DNA.
DR PIR; T43943; T43943.
DR RefSeq; WP_011499240.1; NC_007955.1.
DR AlphaFoldDB; O93632; -.
DR SMR; O93632; -.
DR STRING; 259564.Mbur_1171; -.
DR EnsemblBacteria; ABE52094; ABE52094; Mbur_1171.
DR GeneID; 3998458; -.
DR KEGG; mbu:Mbur_1171; -.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 1642at2157; -.
DR Proteomes; UP000001979; 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_0000091031"
FT DOMAIN 19..229
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 596
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 730 AA; 80478 MW; 3C4676FEB84E6E40 CRC64;
MGRRKKMVER VTALMSNPLM IRNIGIVAHI DHGKTTLSDN LLAGAGMISK ELAGRQLFMD
SDAEEQERGI TIDSSNVSMV HEYEGKEYLI NLIDTPGHVD FGGDVTRAMR AVDGAVVVID
AVEGTMPQTE TVLRQALKEH VKPVLFINKV DRLINELQVD DQEMQIRLGK LIDHVNKLIK
GMNEERYNAG WRVDAAEGTV AFGSALYNWA ISVPMMKKTG VSFSEVFNYC REEDMKSLAE
KCPLHEAVND MVIRFLPSPI DAQKGRVGAI WHGDHESGIG KQMSVADAKG DVAFMVTDIS
MDPHAGEVST GRLFSGSLSR GMEVYVSGAS KTNRIQQVGV FMGPERLEVD AIPAGNIAAV
TGLRDAFVGA TVTTLEGMEP FESIKHASEP VVTVAVEAKH MKDLPKLVEV LRQVAKEDPT
LKITLDEETG EHLMAGMGEL HLEVIAHRIE RDKGVEITTT PPLVVYRETI TGTAGPVEGK
SPNRHNRFYV IVEPLEPEVR ELIRNDEISM RMPEVERREK LMAAGLNKDE AKKIVNIFES
NAYFDMTKGI QYLNETMELI IEGFTEVMKA GPLSKEPCMG VKVKLMDAKL HEDAVHRGPA
QVIPASRQAI QAAMLMADDT LFEPYQKVFI QVPQEQMGGA TKEIQGRRGV IIDMTSEGDT
TVIESKAPVS ELFGFAGDIR SATEGRAMWS TEFAGFEPLP MSLMTEVVTG IRKRKGLKAA
LPQAEDFMSM
