EFG_THET2
ID EFG_THET2 Reviewed; 691 AA.
AC Q72I01;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=TT_C1331;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS81673.1; -; Genomic_DNA.
DR RefSeq; WP_011173716.1; NC_005835.1.
DR PDB; 4V9J; X-ray; 3.86 A; AY/CY=4-690.
DR PDB; 4V9K; X-ray; 3.50 A; AY/CY=4-690.
DR PDB; 4V9L; X-ray; 3.50 A; AY/CY=4-690.
DR PDB; 4V9M; X-ray; 4.00 A; AY/CY=4-690.
DR PDB; 4W29; X-ray; 3.80 A; AY/CY=4-690.
DR PDBsum; 4V9J; -.
DR PDBsum; 4V9K; -.
DR PDBsum; 4V9L; -.
DR PDBsum; 4V9M; -.
DR PDBsum; 4W29; -.
DR AlphaFoldDB; Q72I01; -.
DR SMR; Q72I01; -.
DR IntAct; Q72I01; 1.
DR STRING; 262724.TT_C1331; -.
DR EnsemblBacteria; AAS81673; AAS81673; TT_C1331.
DR KEGG; tth:TT_C1331; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_0; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000000592; 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; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
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_B; EF_G_EF_2_B; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
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; IPR004540; Transl_elong_EFG/EF2.
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; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..691
FT /note="Elongation factor G"
FT /id="PRO_0000091247"
FT DOMAIN 10..284
FT /note="tr-type G"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 56..61
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4V9L"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4V9L"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 416..420
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:4V9L"
FT STRAND 444..456
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 457..469
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 540..544
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 545..550
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 579..595
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 601..608
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 615..626
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:4V9K"
FT TURN 650..654
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 656..662
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:4V9K"
FT STRAND 671..677
FT /evidence="ECO:0007829|PDB:4V9K"
FT HELIX 682..686
FT /evidence="ECO:0007829|PDB:4V9K"
SQ SEQUENCE 691 AA; 76911 MW; 109D07619C9EEC81 CRC64;
MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA TMDFMEQERE
RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV LDGAIVVFDS SQGVEPQSET
VWRQAEKYHV PRIAFANKMD KTGADLWLVI RTMQERLGAR PVVMQLPIGR EDTFSGIIDV
LRMKAYTYGN DLGTDIREIP IPEEYLDQAR EYHEKLVEVA ADFDEHIMLK YLEGEEPTEE
ELVAAIRKGT IDLKITPVFL GSALKNKGVQ LLLDAVVDYL PSPLDIPPIK GTTPEGEVVE
IHPDPNGPLA ALAFKIMADP YVGRLTFIRV YSGTLTSGSY VYNTTKGRKE RVARLLRMHA
NHREEVEELK AGDLGAVVGL KETITGDTLV GEDAPRVILE SIEVPEPVID VAIEPKTKAD
QEKLSQALAR LAEEDPTFRV STHPETGQTI ISGMGELHLE IIVDRLKREF KVDANVGKPQ
VAYRETITKP VDVEGKFIRQ TGGRGQYGHV KIKVEPLPRG SGFEFVNAIV GGVIPKEYIP
AVQKGIEEAM QSGPLIGFPV VDIKVTLYDG SYHEVDSSEM AFKIAGSMAI KEAVQKGDPV
ILEPIMRVEV TTPEEYMGDV IGDLNARRGQ ILGMEPRGNA QVIRAFVPLA EMFGYATDLR
SKTQGRGSFV MFFDHYQEVP KQVQEKLIKG Q
