ID A0A023D9R8_9BACI Unreviewed; 609 AA.
AC A0A023D9R8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Elongation factor 4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000256|HAMAP-Rule:MF_00071,
GN ECO:0000313|EMBL:GAJ38128.1};
GN ORFNames=GCA01S_001_00720 {ECO:0000313|EMBL:GAJ38128.1};
OS Parageobacillus caldoxylosilyticus NBRC 107762.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=1220594 {ECO:0000313|EMBL:GAJ38128.1, ECO:0000313|Proteomes:UP000023561};
RN [1] {ECO:0000313|EMBL:GAJ38128.1, ECO:0000313|Proteomes:UP000023561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107762 {ECO:0000313|EMBL:GAJ38128.1,
RC ECO:0000313|Proteomes:UP000023561};
RA Hosoyama A., Hosoyama Y., Katano-Makiyama Y., Tsuchikane K., Ohji S.,
RA Ichikawa N., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Geobacillus caldoxylosilyticus NBRC
RT 107762.";
RL Submitted (APR-2014) 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:0000256|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:0000256|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00071};
CC Cytoplasmic side {ECO:0000256|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:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_00071}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAJ38128.1}.
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DR EMBL; BAWO01000001; GAJ38128.1; -; Genomic_DNA.
DR RefSeq; WP_017435619.1; NZ_BAWO01000001.1.
DR AlphaFoldDB; A0A023D9R8; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000023561; Unassembled WGS sequence.
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; cd03699; EF4_II; 1.
DR CDD; cd16260; EF4_III; 1.
DR CDD; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW Elongation factor {ECO:0000313|EMBL:GAJ38128.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00071};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00071};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00071};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00071}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071};
KW Reference proteome {ECO:0000313|Proteomes:UP000023561}.
FT DOMAIN 11..193
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 23..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 609 AA; 68426 MW; 01192AEF9AE7E030 CRC64;
MNREERLKRR DRIRNFSIIA HIDHGKSTLA DRILEKTGAL SEREMREQML DSMDLERERG
ITIKLNAVQL KYKAKDGEEY IFHLIDTPGH VDFTYEVSRS LAACEGAILV VDAAQGIEAQ
TLANVYLAID NNLEILPVIN KIDLPSAEPE RVRQEIEEVI GLDASDAVLA SAKVGIGIEE
ILEKIVEKIP APSGDPDAPL KALIFDSLYD SYRGVVAYIR VVDGTVKPGQ RIKMMSTGKE
FEVVEVGVFT PKPKQVDELT VGDVGYLTAS IKNVSDTRVG DTITDAENPA SEPLPGYRKL
NPMVFCGMYP IDTARYNDLR EALEKLQLND AALYFEPETS QALGFGFRCG FLGLLHMEIV
QERIEREFNI DLITTAPSVV YKVHLTDGTE VEVDNPSNMP EPQKIDHVEE PYVKATIMVP
NDYVGPVMEL CQAKRGNFVD MQYLDEKRVT LIYDIPLSEI VYDFFDTLKS STKGYASFDY
ELIGYKPSNL VKMDILLNGE KIDALSFIVH RDAAYERGKV IVEKLKDLIP RQQFEVPVQA
AIGNKIIARS TIKALRKNVL AKCYGGDVSR KRKLLEKQKE GKKRMKQIGS VEVPQEAFMA
VLKIDDNKK
//
