LEPA_AQUAE
ID LEPA_AQUAE Reviewed; 600 AA.
AC O67618;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=aq_1725;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GTP.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structures of GTP-binding protein lepA from Aquifex aeolicus.";
RL Submitted (FEB-2009) to the PDB data bank.
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; AE000657; AAC07583.1; -; Genomic_DNA.
DR PIR; H70448; H70448.
DR RefSeq; NP_214184.1; NC_000918.1.
DR RefSeq; WP_010881121.1; NC_000918.1.
DR PDB; 2YWE; X-ray; 2.05 A; A=1-600.
DR PDB; 2YWF; X-ray; 2.24 A; A=1-600.
DR PDB; 2YWG; X-ray; 2.94 A; A=1-600.
DR PDB; 2YWH; X-ray; 2.24 A; A=1-600.
DR PDBsum; 2YWE; -.
DR PDBsum; 2YWF; -.
DR PDBsum; 2YWG; -.
DR PDBsum; 2YWH; -.
DR AlphaFoldDB; O67618; -.
DR SMR; O67618; -.
DR STRING; 224324.aq_1725; -.
DR EnsemblBacteria; AAC07583; AAC07583; aq_1725.
DR KEGG; aae:aq_1725; -.
DR PATRIC; fig|224324.8.peg.1326; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_0; -.
DR InParanoid; O67618; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 182107at2; -.
DR EvolutionaryTrace; O67618; -.
DR Proteomes; UP000000798; 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; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
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..600
FT /note="Elongation factor 4"
FT /id="PRO_0000176223"
FT DOMAIN 4..186
FT /note="tr-type G"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071,
FT ECO:0000269|Ref.2"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071,
FT ECO:0000269|Ref.2"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:2YWE"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2YWG"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2YWG"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:2YWE"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 207..219
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:2YWE"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 238..250
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2YWF"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:2YWE"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 400..415
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 432..440
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 452..466
FT /evidence="ECO:0007829|PDB:2YWE"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 472..482
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 485..496
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:2YWE"
FT HELIX 509..523
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:2YWE"
FT STRAND 540..547
FT /evidence="ECO:0007829|PDB:2YWE"
SQ SEQUENCE 600 AA; 67657 MW; EA69B32A062D3081 CRC64;
MEQKNVRNFC IIAHVDHGKS TLADRLLEYT GAISEREKRE QLLDTLDVER ERGITVKMQA
VRMFYKAKDG NTYKLHLIDT PGHVDFSYEV SRALAACEGA LLLIDASQGI EAQTVANFWK
AVEQDLVIIP VINKIDLPSA DVDRVKKQIE EVLGLDPEEA ILASAKEGIG IEEILEAIVN
RIPPPKGDPQ KPLKALIFDS YYDPYRGAVA FVRIFDGEVK PGDKIMLMST GKEYEVTEVG
AQTPKMTKFD KLSAGDVGYI AASIKDVRDI RIGDTITHAK NPTKEPVPGF QPAKPMVYAG
IYPAEDTTYE ELRDALEKYA INDAAIVYEP ESSPALGMGF RVGFLGLLHM EIVQERLERE
YGVKIITTAP NVIYRVKKKF TDEVIEVRNP MDFPDNAGLI EYVEEPFVLV TIITPKEYVG
PIIQLCQEKR GIQKNMTYLD PNTVYLEYEM PLSEIIVDFH DKIKSISRGF ASYDYEFIGY
RPSDLIKLTV LINKKPVDAL SFIVHADRAQ KFARRVAEKL RETIPRQLFE VHIQVAKGGK
VIASERIKPL RANVTAKCYG GDVTRKKKLL ENQKEGKKRM KQFGKVQLPQ EAFLSVLKVE
