ID A0A0C1KDV8_9BACT Unreviewed; 602 AA.
AC A0A0C1KDV8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:KIC77162.1};
GN ORFNames=DB41_CW00110 {ECO:0000313|EMBL:KIC77162.1};
OS Neochlamydia sp. TUME1.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478174 {ECO:0000313|EMBL:KIC77162.1, ECO:0000313|Proteomes:UP000031320};
RN [1] {ECO:0000313|EMBL:KIC77162.1, ECO:0000313|Proteomes:UP000031320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUME1 {ECO:0000313|EMBL:KIC77162.1,
RC ECO:0000313|Proteomes:UP000031320};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
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:KIC77162.1}.
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DR EMBL; JRXI01000013; KIC77162.1; -; Genomic_DNA.
DR RefSeq; WP_039383287.1; NZ_JRXI01000013.1.
DR AlphaFoldDB; A0A0C1KDV8; -.
DR PATRIC; fig|1478174.3.peg.153; -.
DR Proteomes; UP000031320; 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; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
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; PF14492; EFG_III; 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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00071}; Elongation factor {ECO:0000313|EMBL:KIC77162.1};
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|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}.
FT DOMAIN 7..189
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 602 AA; 67486 MW; 31EEBE9B8B986295 CRC64;
MVSYNRKNIR NFSIIAHIDH GKSTIADRLI ELTHTVSKRE MQEQLLDDMD LERERGITIK
AHPVTMNYQA ENGQIYQINL IDTPGHVDFT YEVSRSLAAC EGALLVVDAA QGVQAQTLAN
VHLAIERDLE IVPVLNKIDL PSADIEGVKQ QIEDVIGLDA SHAICCSAKS GIGIETILER
IINDVPAPKE PVDDLLRALV FDSHYDNYRG VMVYIRVISG EIRKGSAIRM MATHKACEVL
EVGKFTPSEK PVETLRSGEV GYMIANIKKT SDVKIGDTIT LQKHPAPDAL PGFKNISPVV
FAGIYPIDST DFEALRDALE KLQLNDSSLH IEQESSMALG FGFRCGFLGL LHLEIIFERI
QREFDLDVIS TAPSVIYKFH LNDTSIKEID NPAHYPDPTH IDYVEEPWVK CHIMIPAEYL
GAIMNLGMDK RGNCIKTETM DARRLLITYR FPLNEIITDF NDKLKSITKG YGSFDYEFDG
YEKSDIIKLE IRVNEEPVDA FSCLVHRSKA ESKGKAICSK LVEVIPMQLF KVPIQAAIGG
KIVARETIRA LTKNVTAKCY GGDITRKRKL WEKQKKGKKR MKEIGKVNIP QSAFMEVLKA
GD
//
