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Database: UniProt
Entry: A0A0A1FDT0_9BURK
LinkDB: A0A0A1FDT0_9BURK
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ID   A0A0A1FDT0_9BURK        Unreviewed;       681 AA.
AC   A0A0A1FDT0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872};
GN   ORFNames=LT85_2797 {ECO:0000313|EMBL:AIY41955.1};
OS   Collimonas arenae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY41955.1, ECO:0000313|Proteomes:UP000030302};
RN   [1] {ECO:0000313|EMBL:AIY41955.1, ECO:0000313|Proteomes:UP000030302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cal35 {ECO:0000313|EMBL:AIY41955.1,
RC   ECO:0000313|Proteomes:UP000030302};
RA   Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT   "Structure and function of bacterial communities in ageing soils: insights
RT   from the Mendocino ecological staircase.";
RL   Soil Biol. Biochem. 69:265-274(2014).
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000256|ARBA:ARBA00005870}.
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DR   EMBL; CP009962; AIY41955.1; -; Genomic_DNA.
DR   RefSeq; WP_038489682.1; NZ_CP009962.1.
DR   AlphaFoldDB; A0A0A1FDT0; -.
DR   STRING; 279058.LT85_2797; -.
DR   KEGG; care:LT85_2797; -.
DR   HOGENOM; CLU_002794_4_1_4; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000030302; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   CDD; cd04088; EFG_mtEFG_II; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 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   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00484; EF-G; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000313|EMBL:AIY41955.1}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000313|EMBL:AIY41955.1}.
FT   DOMAIN          9..281
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   681 AA;  71571 MW;  15783E853B351A2F CRC64;
     MTATTTLRAN SRNFGIIAHI DAGKTTLSER ILLKTGEIHR AGEVHDGAAT MDHMDLEKER
     GITIGAAATR AVWNGHTFTL IDTPGHIDFA IEVERSLRVL DGAIAVLSGV EGIQPQTETV
     WRQAQKHAVP MIVFVNKMDR VGADFERVVG QMRDRLDALP VPLTIPVGAA DTFAGAIDVL
     GQRLLSWDAS GLMTSSALPQ NLAAIALDAY AHAAAVAADA SDALTSAYLD NDTLSAIEIA
     TGLRAMTIAR RAVPVFAGSA YKNAGIEPLL DAIVDWLPSP EERAAPTGLL AGASVSVGTS
     PSDPLAALVF KVIHDDHGSL SFVRLYGGTL REGDTVWNAT LGAPVRIGRL YVVHADRRVG
     VEEASAGSII AIAGLKDALT GQTLSTKAVP LTLETIQAGE PVVALAVEPA NGGDRSKMIV
     ALDRFRREDP SLRLESNPET GETVLWGQGE LHLDVVLERV RREAGVDVKA GAPHVAYKET
     IDGPAVQVEG KVSKQNGGKG QYARVVLRVE PFDGAFAFEN AVKGGAIPSA FFPAVEKGVR
     QALAQGPLGQ PVTGVKVTLL DGDHHAVDSS DMTFTVAAKD GVLAGLKRAH PVLLEPVMTV
     TVDAPTANAG DVIGDLQRRS GRVLGIEDHA GRVEIVGEVP LARLFGHTTD LRSLSQGRAF
     ASAVYARHAA SASSHTEAIA A
//
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