ID EF2_HALMA Reviewed; 728 AA.
AC Q5UZS7; E3VNY5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
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};
GN Synonyms=ef-2 {ECO:0000303|PubMed:21296924}; OrderedLocusNames=rrnAC2413;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-379.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=21296924; DOI=10.1099/ijs.0.029298-0;
RA Papke R.T., White E., Reddy P., Weigel G., Kamekura M., Minegishi H.,
RA Usami R., Ventosa A.;
RT "A multilocus sequence analysis approach to the phylogeny and taxonomy of
RT the Halobacteriales.";
RL Int. J. Syst. Evol. Microbiol. 61:2984-2995(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY596297; AAV47226.1; -; Genomic_DNA.
DR EMBL; HQ149393; ADP09119.1; -; Genomic_DNA.
DR RefSeq; WP_004959082.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UZS7; -.
DR SMR; Q5UZS7; -.
DR STRING; 272569.rrnAC2413; -.
DR PaxDb; 272569-rrnAC2413; -.
DR EnsemblBacteria; AAV47226; AAV47226; rrnAC2413.
DR GeneID; 64824335; -.
DR KEGG; hma:rrnAC2413; -.
DR PATRIC; fig|272569.17.peg.3027; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR Proteomes; UP000001169; Chromosome I.
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; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR CDD; cd01514; Elongation_Factor_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00490; aEF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 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..728
FT /note="Elongation factor 2"
FT /id="PRO_0000091028"
FT DOMAIN 19..261
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 596
FT /note="Diphthamide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT CONFLICT 233
FT /note="A -> N (in Ref. 2; ADP09119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 80418 MW; 3DE067B7B14C3ECE CRC64;
MGRRKKIVQE CETLMDDPEH IRNIAIAAHV DHGKTTLTDN LLAGAGMISD DTAGEQLAMD
TEEDEQERGI TIDAANVSMT HEYEDQNHLI NLIDTPGHVD FGGDVTRAMR AVDGALVVVD
AVEGAMPQTE TVLRQALREG VKPTLFINKV DRLISELQEG PEEMQKRLLA VIQDVNDLIR
GMTEEMDDIE DWTVSVEEGT VGFGSALYKW GVSMPSMQRT GMDFGEIMEL ERADNRQELH
ERTPLSDVVL DMVCEHFPNP VDAQPMRVPR IWRGDAESQL ADDMRLVNED GEVVLMVTDI
GVDPHAGEIA AGRVFSGTLE KGQELYVSGT AGKNRIQSVG IYMGGEREEV DRVPAGNIAA
VTGLKDAIAG STVSSEEMTP FESIEHISEP VITKSVEAQN MDDLPKLIET LQQVAKEDPT
IQVEINEDTG EHLISGQGEL HLEVIGQRIE RNQGIPINTG EPIVVYREAP QEDSREVEGR
SPNNHNRFYI SIEPLGEDIV ETIKMGEASM DMPELERREA LQEAGMDKDD SQNIEHIHGT
NILLDETKGI QHLNETMELV IEGLEEALDD GPLASEPVQG SLIRLHDARL HEDAIHRGPA
QVIPAVREAV HNSLIDASIK LLEPIQQVRI DVPNDHMGAA SGEIQGRRGR VDDMYQEGDL
MVVEGVAPVD EMIGFSSDIR SATEGRASWN TENAGFQVLA DNLQPDKISE IRERKGMKQE
LNPAIDYF
//
