EFG_THET8
ID EFG_THET8 Reviewed; 691 AA.
AC Q5SHN5;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=TTHA1695;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2587224; DOI=10.1093/nar/17.21.8863;
RA Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.;
RT "Nucleotide sequence of the Thermus thermophilus HB8 gene coding for
RT elongation factor G.";
RL Nucleic Acids Res. 17:8863-8863(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=2362824; DOI=10.1093/nar/18.12.3659;
RA Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.;
RT "Nucleotide sequence of the Thermus thermophilus HB8 rps12 and rps7 genes
RT coding for the ribosomal proteins S12 and S7.";
RL Nucleic Acids Res. 18:3659-3659(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8070396; DOI=10.1002/j.1460-2075.1994.tb06675.x;
RA Czworkowski J., Wang J., Steitz T.A., Moore P.B.;
RT "The crystal structure of elongation factor G complexed with GDP, at 2.7-A
RT resolution.";
RL EMBO J. 13:3661-3668(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS).
RX PubMed=8070397; DOI=10.1002/j.1460-2075.1994.tb06676.x;
RA Aevarsson A., Brazhnikov E., Garber M., Zheltonosova J., Chirgadze Y.,
RA Al-Karadaghi S., Svensson L.A., Liljas A.;
RT "Three-dimensional structure of the ribosomal translocase: elongation
RT factor G from Thermus thermophilus.";
RL EMBO J. 13:3669-3677(1994).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X16278; CAA34354.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71518.1; -; Genomic_DNA.
DR EMBL; X52165; CAA36420.1; -; Genomic_DNA.
DR PIR; S15928; EFTWG.
DR RefSeq; WP_011228848.1; NC_006461.1.
DR RefSeq; YP_144961.1; NC_006461.1.
DR PDB; 1DAR; X-ray; 2.40 A; A=1-691.
DR PDB; 1EFG; X-ray; 2.70 A; A=1-691.
DR PDB; 1ELO; X-ray; 2.80 A; A=1-691.
DR PDB; 1ZN0; EM; 15.50 A; B=6-688.
DR PDB; 2EFG; X-ray; 2.60 A; A=1-691.
DR PDB; 4V5F; X-ray; 3.60 A; AY/CY=1-691.
DR PDB; 4V5M; EM; 7.80 A; AY=1-691.
DR PDB; 4V5N; EM; 7.60 A; AY=1-691.
DR PDB; 4V8U; X-ray; 3.70 A; AY/CY=1-691.
DR PDB; 4V90; X-ray; 2.95 A; AY=1-691.
DR PDB; 4V9H; X-ray; 2.86 A; AY=10-689.
DR PDB; 4WPO; X-ray; 2.80 A; BZ/DZ=8-691.
DR PDB; 4WQF; X-ray; 2.80 A; BZ/DZ=8-691.
DR PDB; 4WQU; X-ray; 2.80 A; BZ/DZ=8-691.
DR PDB; 4WQY; X-ray; 2.80 A; BZ/DZ=8-691.
DR PDB; 5HAU; X-ray; 3.00 A; 1z/2z=8-691.
DR PDB; 5OT7; EM; 3.80 A; U=4-690.
DR PDB; 6UCQ; X-ray; 3.50 A; 1v/2v=8-691.
DR PDBsum; 1DAR; -.
DR PDBsum; 1EFG; -.
DR PDBsum; 1ELO; -.
DR PDBsum; 1ZN0; -.
DR PDBsum; 2EFG; -.
DR PDBsum; 4V5F; -.
DR PDBsum; 4V5M; -.
DR PDBsum; 4V5N; -.
DR PDBsum; 4V8U; -.
DR PDBsum; 4V90; -.
DR PDBsum; 4V9H; -.
DR PDBsum; 4WPO; -.
DR PDBsum; 4WQF; -.
DR PDBsum; 4WQU; -.
DR PDBsum; 4WQY; -.
DR PDBsum; 5HAU; -.
DR PDBsum; 5OT7; -.
DR PDBsum; 6UCQ; -.
DR AlphaFoldDB; Q5SHN5; -.
DR SMR; Q5SHN5; -.
DR IntAct; Q5SHN5; 52.
DR STRING; 300852.55773077; -.
DR EnsemblBacteria; BAD71518; BAD71518; BAD71518.
DR GeneID; 3169680; -.
DR KEGG; ttj:TTHA1695; -.
DR PATRIC; fig|300852.9.peg.1665; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_0; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; Q5SHN5; -.
DR EvolutionaryTrace; Q5SHN5; -.
DR PRO; PR:Q5SHN5; -.
DR Proteomes; UP000000532; 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; Reference proteome.
FT CHAIN 1..691
FT /note="Elongation factor G"
FT /id="PRO_0000091249"
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:0000250"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1ELO"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1ELO"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 323..338
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 426..433
FT /evidence="ECO:0007829|PDB:1ELO"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1ELO"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:1ELO"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:1ELO"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 491..499
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 506..516
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 539..549
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 562..570
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 579..595
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 600..612
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 614..618
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 619..626
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 631..637
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 640..648
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 655..662
FT /evidence="ECO:0007829|PDB:1DAR"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:1DAR"
FT STRAND 668..678
FT /evidence="ECO:0007829|PDB:1DAR"
FT HELIX 681..688
FT /evidence="ECO:0007829|PDB:1DAR"
SQ SEQUENCE 691 AA; 76879 MW; 8F0063EE8123470E CRC64;
MAVKVEYDLK RLRNIGIAAH IDAGKTTTTE RILYYTGRIH KIGEVHEGAA TMDFMEQERE
RGITITAAVT TCFWKDHRIN IIDTPGHVDF TIEVERSMRV LDGAIVVFDS SQGVEPQSET
VWRQAEKYKV PRIAFANKMD KTGADLWLVI RTMQERLGAR PVVMQLPIGR EDTFSGIIDV
LRMKAYTYGN DLGTDIREIP IPEEYLDQAR EYHEKLVEVA ADFDENIMLK 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
