ID L8XXK0_9GAMM Unreviewed; 596 AA.
AC L8XXK0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ORFNames=F387_00170 {ECO:0000313|EMBL:ELV08778.1};
OS Wohlfahrtiimonas chitiniclastica SH04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Wohlfahrtiimonas.
OX NCBI_TaxID=1261130 {ECO:0000313|EMBL:ELV08778.1, ECO:0000313|Proteomes:UP000011617};
RN [1] {ECO:0000313|EMBL:ELV08778.1, ECO:0000313|Proteomes:UP000011617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH04 {ECO:0000313|EMBL:ELV08778.1,
RC ECO:0000313|Proteomes:UP000011617};
RX PubMed=23558531;
RA Cao X.M., Chen T., Xu L.Z., Yao L.S., Qi J., Zhang X.L., Yan Q.L.,
RA Deng Y.H., Guo T.Y., Wang J., Hu K.X., Xu B.L.;
RT "Complete Genome Sequence of Wohlfahrtiimonas chitiniclastica Strain SH04,
RT Isolated from Chrysomya megacephala Collected from Pudong International
RT Airport in China.";
RL Genome Announc. 1:E0011913-E0011913(2013).
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:ELV08778.1}.
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DR EMBL; AOBV01000002; ELV08778.1; -; Genomic_DNA.
DR RefSeq; WP_008314640.1; NZ_KB372778.1.
DR AlphaFoldDB; L8XXK0; -.
DR GeneID; 58263062; -.
DR PATRIC; fig|1261130.3.peg.374; -.
DR HOGENOM; CLU_009995_3_3_6; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000011617; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 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 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 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:ELV08778.1};
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:UP000011617}.
FT DOMAIN 2..184
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 596 AA; 66108 MW; BF60EE36109058D1 CRC64;
MKNIRNFSII AHIDHGKSTI ADRFIQICDG LSEREMEAQV LDSMDIERER GITIKAHSVS
LDYKAKNGEV YHLNFIDTPG HVDFSYEVSR SLFACEGALL VVDAAQGVEA QSVANCYTAI
DHGLEVVPVL NKIDLPAADP MKVAAEIEDI IGIEAMDAVT CSAKTGMGVE DVLETLVQKI
PAPKGDPNAP LKALIIDSWF DPYVGVISLV RIFEGTLRVR DKMQVMSTKR NYQVSHVGVF
TPKRLDKTEL SAGQVGFVIA GIKEIDGVPV GDTLTLENNP ATEAVPGFQK VQSRVFSGLF
PVDSSDYENL REALQKLRLN DASLNFEPES SQALGFGFRC GFLGMLHMEI IQERLEREYD
LDLITTAPTV IYELEKTDGE VVLIDNPNDL PAPNKISEIR EPIIRANILT PQEYLGNIIT
LCVEKRGVQK NIVYAGSQVQ LQFELPMSEV VLDFFDRLKS VSRGYASFDY EFVRYEAANL
AKVDILINGE TVDALALIVH KDNAVYRGRD LVEKMKELIP RQMFDIAIQA AIGAQIIARS
TVKAMRKDVL AKCYGGDVSR KRKLLEKQKA GKKRMKQVGN VEIPQSAFLA VLQVDK
//
