ID K2BVH8_9BACT Unreviewed; 404 AA.
AC K2BVH8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Elongation factor EFG domain-containing protein {ECO:0000259|SMART:SM00838};
DE Flags: Fragment;
GN ORFNames=ACD_42C00297G0001 {ECO:0000313|EMBL:EKD77551.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD77551.1};
RN [1] {ECO:0000313|EMBL:EKD77551.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD77551.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMFJ01017568; EKD77551.1; -; Genomic_DNA.
DR AlphaFoldDB; K2BVH8; -.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03699; EF4_II; 1.
DR CDD; cd16260; EF4_III; 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; 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; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR01393; lepA; 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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF50447; Translation proteins; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 205..292
FT /note="Elongation factor EFG"
FT /evidence="ECO:0000259|SMART:SM00838"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD77551.1"
SQ SEQUENCE 404 AA; 44921 MW; B031F38C333DAC51 CRC64;
LIIDSWFDSY LGVVSLVRVK QGTLKIGDKI RVMSTGRDHI VDGVGIFTPK RFPLQQLCAG
EVGYVVAGIK DIFGAPVGDT LTHAKNAATT PLPGFKKVKP QVYAGMFPIS ADDYEAFREA
LSKLRLNDAA LFYEPENSSA LGAGFRCGFL GLLHMEIVQE RLEREYDLDL ITTAPTVVYE
LLMKNSEVIY IDNPSQLPEI SAIAELREPI AEVNILTPQE YVGSIITLCI ERRGIQKKMI
YVGNQVSLQY QIPLSEVVSD FFDRLKSLSR GFASLDYSFD HFIEANLVKL DILVNGDKVD
ALASIVHRDH AESRGRDIAE RLQSIIPRQM YDVALQATIG GKIIARSTVK ALRKNVTAKC
YGGDVTRKKK LLEKQKAGKK RMKQIGKVTI PQDAFLAVLR SDKK
//
