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Database: UniProt
Entry: A0A343JFI4_9CLOT
LinkDB: A0A343JFI4_9CLOT
Original site: A0A343JFI4_9CLOT 
ID   A0A343JFI4_9CLOT        Unreviewed;       690 AA.
AC   A0A343JFI4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Translation elongation factor G {ECO:0000313|EMBL:ASW44292.1};
GN   ORFNames=BEN51_12785 {ECO:0000313|EMBL:ASW44292.1};
OS   Clostridium isatidis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=182773 {ECO:0000313|EMBL:ASW44292.1, ECO:0000313|Proteomes:UP000264883};
RN   [1] {ECO:0000313|EMBL:ASW44292.1, ECO:0000313|Proteomes:UP000264883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15098 {ECO:0000313|EMBL:ASW44292.1,
RC   ECO:0000313|Proteomes:UP000264883};
RA   Little G.T., Minton N.P.;
RT   "Complete Genome Sequence Of The Indigo Reducing Clostridium isatidis
RT   DSM15098.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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; CP016786; ASW44292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A343JFI4; -.
DR   KEGG; cia:BEN51_12785; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000264883; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd04170; EF-G_bact; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 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; IPR047872; EFG_IV.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
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   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:0000313|EMBL:ASW44292.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ASW44292.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264883}.
FT   DOMAIN          7..279
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   690 AA;  76842 MW;  539EC425193EF58F CRC64;
     MKSYRVDNIR NVGLIGHSSV GKTSLVEALL YSNGNIDRLG KVEEGTTVSD FDPEEKRRNI
     SISVSIESTE INDTKINLID IPGYFDFSGE LIQGMRAADV ATIVVSGVSG VQVGTEKAWD
     YCNKIKLPRA FFINKLDREN SSYERTLEEL KSKFGISVVP LQFPIGSEEN LKGIVNVISG
     KAIIYDEKNN YREIDAPEDI KDKIDEYKNI IMEAVAETSE EYLEKYFSEG ELTNEDIYTG
     LVKGCASGDI APVMCGSSLK VIGMKSFLED IVSCFPSPRY AIAQKAKELE SEKEIFVNFD
     ETKLFSALVF KTIADPFVGK ISLFKVITGE LSNEVSVINS NKGKVEKISN IFFMNGKNQA
     QTKKVIAGDI AAVSKLQYTE TGDTLCDVNY KLVYDKMNFP RTNISMAILP LAKNDEDKIS
     IVLQRLQEED PTFRVERDVE NAETIISGIG ETHLEVIASK IKNKYGVEVI LRAPKIPYRE
     TIKGMAYVQG KHKKQSGGHG QYGDVKIQFE PRNDGETDLE FVDSIVGGVV PRNFIPAVEK
     GLRESIEKGV LAGYPVIGLK ATLKDGSYHT VDSSEMAFKM ATYIAYKKGL EQAKPVLLEP
     IMSLEVIIPE ENMGDVIGDI NKRRGRVIGM EPYEKLQKII AEVPMAEITK YSTDLSSMTQ
     ARGSFKAEFL RYEEVPDNIA KKIIEEAKRN
//
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