ID   EF2_PYRNV               Reviewed;         740 AA.
AC   B1YE08;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Tneu_1090;
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS   V24Sta) (Thermoproteus neutrophilus).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=444157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001014; ACB40021.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1YE08; -.
DR   SMR; B1YE08; -.
DR   STRING; 444157.Tneu_1090; -.
DR   EnsemblBacteria; ACB40021; ACB40021; Tneu_1090.
DR   KEGG; tne:Tneu_1090; -.
DR   eggNOG; arCOG01559; Archaea.
DR   HOGENOM; CLU_002794_11_1_2; -.
DR   OMA; GVMTQTE; -.
DR   Proteomes; UP000001694; 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; 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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..740
FT                   /note="Elongation factor 2"
FT                   /id="PRO_1000091772"
FT   DOMAIN          23..264
FT                   /note="tr-type G"
FT   BINDING         32..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         98..102
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         152..155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   MOD_RES         605
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   740 AA;  83056 MW;  C67AE5E7548E5AD4 CRC64;
     MSSAVRVVEK QLDEILAIAR NPAQIRNAGT LAHVDHGKTT TSDSLLMGAG LLSPKVAGKA
     LAMDYVPIEQ LRQMTVKAAN ISLYFEYGGK PYLINFVDTP GHVDFTGHVT RSLRVMDGGL
     VVVDAVEGVM TQTETVVRQA LEEYVRPVLF INKIDRLIKE LRLSPQEIQQ RILTIVKDFN
     ALIDMFAPPE FKDKWKVDPG KGQMAMGSAL HKWGITIPMA QKAGIKFSNI VDAYEKGYVD
     QLAQEFPLYK TLLTMIIEHV PPPNVAQKYR IPRLWRGDLN SEIGKALLEA DPNGPTVIAV
     SKVNKDPHAG LIATGRVFSG TIREGDEIYI IGRKMKKKVL QTYIYMGPSR IIVPYMPAGN
     IVALMGVDEA RAGDTLVDPR LSEIPPFEKM RYISEPVVTV AIEPKNPAEL ARLVEALKDL
     VIEDPTLDLK IDQETGQILL SGVGTLHLEI ATWLLKERTK TEFTVSPPLI RFRETVRERS
     QVWEGKSPNK HNRLYFYVEP LDETTIELIA TREITEDQDP RERAKILREK AGWDADEARG
     IWAIDDRFFN LIVDRTSGIQ YLREIRDYIV QGFRWATEAG PLAQEPMRGL KVVLTDAVVH
     EDPAHRGPAQ IMPATKNAIF AAVLSARPTI LEPLMKLDIK VAPDYIGAVT SVLNKHRGKI
     LDMTQQEYMA YLRAELPVLE SFTISDELRA AAAGKIFWSM QFSRWAPMPE SILADMVKQL
     RKKKGLKEEI PKPTDFVEAF