LEPA_THET8
ID LEPA_THET8 Reviewed; 610 AA.
AC Q5SKA7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; OrderedLocusNames=TTHA0741;
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 [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.
CC -!- FUNCTION: Required for accurate and efficient protein synthesis under
CC certain stress conditions. May act as a fidelity factor of the
CC translation reaction, by catalyzing a one-codon backward translocation
CC of tRNAs on improperly translocated ribosomes. Back-translocation
CC proceeds from a post-translocation (POST) complex to a pre-
CC translocation (PRE) complex, thus giving elongation factor G a second
CC chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-
CC dependent manner. {ECO:0000255|HAMAP-Rule:MF_00071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00071}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00071}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00071}.
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DR EMBL; AP008226; BAD70564.1; -; Genomic_DNA.
DR RefSeq; WP_011228160.1; NC_006461.1.
DR RefSeq; YP_144007.1; NC_006461.1.
DR PDB; 4W2E; X-ray; 2.90 A; y=6-610.
DR PDB; 5IMQ; EM; 3.80 A; B=1-610.
DR PDB; 5IMR; EM; -; C=1-610.
DR PDB; 5J8B; X-ray; 2.60 A; z=6-610.
DR PDBsum; 4W2E; -.
DR PDBsum; 5IMQ; -.
DR PDBsum; 5IMR; -.
DR PDBsum; 5J8B; -.
DR AlphaFoldDB; Q5SKA7; -.
DR SMR; Q5SKA7; -.
DR STRING; 300852.55772123; -.
DR EnsemblBacteria; BAD70564; BAD70564; BAD70564.
DR GeneID; 3170109; -.
DR KEGG; ttj:TTHA0741; -.
DR PATRIC; fig|300852.9.peg.734; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_0; -.
DR OMA; MVQIAIQ; -.
DR PhylomeDB; Q5SKA7; -.
DR BRENDA; 3.6.5.3; 2305.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.2570; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
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; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43512; PTHR43512; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 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; Cell inner membrane; Cell membrane; GTP-binding; Hydrolase;
KW Membrane; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..610
FT /note="Elongation factor 4"
FT /id="PRO_0000224806"
FT DOMAIN 7..189
FT /note="tr-type G"
FT BINDING 19..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4W2E"
FT TURN 91..95
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4W2E"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:4W2E"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 351..365
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 456..471
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 501..508
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 510..524
FT /evidence="ECO:0007829|PDB:4W2E"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:4W2E"
FT STRAND 544..551
FT /evidence="ECO:0007829|PDB:4W2E"
FT TURN 558..561
FT /evidence="ECO:0007829|PDB:4W2E"
FT HELIX 567..586
FT /evidence="ECO:0007829|PDB:4W2E"
FT TURN 596..601
FT /evidence="ECO:0007829|PDB:4W2E"
SQ SEQUENCE 610 AA; 67600 MW; BC2CD051542C0E78 CRC64;
MVRMDLSRIR NFSIIAHVDH GKSTLADRIL ELTHAVSDRE MREQFLDSLE LERERGITIK
ASAVRVTYRA KDGEEYVFHL IDTPGHVDFT YEVSRALAAV EGVLLVVDAS QGVEAETLAK
FYMALEHGHV IIPVINKIDL PNARPLEVAL EVEEVLGLPA DEAIFASGKT GEGVEEILEA
IVQRIPPPKG DPEAPLKALI FDSVYDAYQG VIPYLRLFEG RVRPGDRIRI YSTGKEFTVD
KVGVFTPQGL VATEALEAGE VGWLVAAIRD IHDVQVGDTI TLADRPTPSP YPGFRPAKPV
VFAGLYPVDS GDYGKLRDAL EKLKLNDAAL TFEPESSTAL GFGFRCGFLG LLHAEIVQER
LEREFGLSLI ATAPSVVYKV RLKSGEEVEV HNPADLPDPT RIEEILEPYV KLTIFTPEEY
VGSLMQLLQE KRGRLVNMNY LPGAQKRVEL VYEAPFAEIL YDFHDRLKSV SRGYASMDYE
QAGYRPGDLV KVNVLVHGEV VDALTFIAHR EKAYTMARAI VDKLAEVIPR QLFEVPIQAA
IGGKIIARAT VKALRKDVLA KCYGGDVTRK KKLLEKQKEG KKRLKAIGKV EVPQEAFLAV
LSAGRDEPKG
