EFG_THETH
ID EFG_THETH Reviewed; 691 AA.
AC P13551;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=fus;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8736554; DOI=10.1016/s0969-2126(96)00061-5;
RA Al-Karadaghi S., Aevarsson A., Garber M., Zheltonosova J., Liljas A.;
RT "The structure of elongation factor G in complex with GDP: conformational
RT flexibility and nucleotide exchange.";
RL Structure 4:555-565(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-573.
RX PubMed=11054294; DOI=10.1006/jmbi.2000.4168;
RA Laurberg M., Kristensen O., Martemyanov K., Gudkov A.T., Nagaev I.,
RA Hughes D., Liljas A.;
RT "Structure of a mutant EF-G reveals domain III and possibly the fusidic
RT acid binding site.";
RL J. Mol. Biol. 303:593-603(2000).
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}.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1KTV. {ECO:0000305}.
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DR RefSeq; WP_011228848.1; NZ_AP019801.1.
DR PDB; 1FNM; X-ray; 2.80 A; A=1-691.
DR PDB; 1JQM; EM; -; B=1-691.
DR PDB; 1JQS; EM; -; B=220-251, C=606-673.
DR PDB; 1KTV; X-ray; 3.80 A; A/B=1-691.
DR PDB; 1PN6; EM; 10.80 A; A=1-691.
DR PDB; 2BCW; EM; 11.20 A; C=200-257.
DR PDB; 2BM0; X-ray; 2.40 A; A=1-691.
DR PDB; 2BM1; X-ray; 2.60 A; A=1-691.
DR PDB; 2BV3; X-ray; 2.50 A; A=1-691.
DR PDB; 2J7K; X-ray; 2.90 A; A=1-691.
DR PDB; 2OM7; EM; 7.30 A; L=1-691.
DR PDB; 3IZP; EM; -; E=1-688.
DR PDB; 4M1K; X-ray; 2.95 A; A=1-691.
DR PDB; 4MYT; X-ray; 3.50 A; A=1-691.
DR PDB; 4MYU; X-ray; 3.00 A; A=1-691.
DR PDBsum; 1FNM; -.
DR PDBsum; 1JQM; -.
DR PDBsum; 1JQS; -.
DR PDBsum; 1KTV; -.
DR PDBsum; 1PN6; -.
DR PDBsum; 2BCW; -.
DR PDBsum; 2BM0; -.
DR PDBsum; 2BM1; -.
DR PDBsum; 2BV3; -.
DR PDBsum; 2J7K; -.
DR PDBsum; 2OM7; -.
DR PDBsum; 3IZP; -.
DR PDBsum; 4M1K; -.
DR PDBsum; 4MYT; -.
DR PDBsum; 4MYU; -.
DR AlphaFoldDB; P13551; -.
DR SMR; P13551; -.
DR DrugBank; DB02703; Fusidic acid.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR GeneID; 3169680; -.
DR BRENDA; 3.6.5.3; 2305.
DR EvolutionaryTrace; P13551; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IMP:CAFA.
DR GO; GO:0005525; F:GTP binding; IDA:CAFA.
DR GO; GO:0003924; F:GTPase activity; IDA:CAFA.
DR GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
DR GO; GO:0043022; F:ribosome binding; IDA:CAFA.
DR GO; GO:0003746; F:translation elongation factor activity; IDA:CAFA.
DR GO; GO:0006414; P:translational elongation; IDA:CAFA.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR DisProt; DP00021; -.
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_0000091248"
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:2BM0"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4M1K"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3IZP"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3IZP"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:3IZP"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2BV3"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3IZP"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3IZP"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2J7K"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 325..336
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 348..358
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:2BM1"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 409..418
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:2BV3"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:1FNM"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:2BM1"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 491..501
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 504..516
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 539..550
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 562..571
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 579..596
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 600..612
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 617..626
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 630..637
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 640..648
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 655..662
FT /evidence="ECO:0007829|PDB:2BM0"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:2BM0"
FT STRAND 668..678
FT /evidence="ECO:0007829|PDB:2BM0"
FT HELIX 681..686
FT /evidence="ECO:0007829|PDB:2BM0"
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
