ID I7IJA9_9BURK Unreviewed; 701 AA.
AC I7IJA9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 50.
DE RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872, ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA2 {ECO:0000313|EMBL:CCG18197.1};
GN Synonyms=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN ORFNames=KUK_0897 {ECO:0000313|EMBL:CCG18197.1};
OS Taylorella equigenitalis 14/56.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Taylorella.
OX NCBI_TaxID=1091497 {ECO:0000313|EMBL:CCG18197.1};
RN [1] {ECO:0000313|EMBL:CCG18197.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=14/56 {ECO:0000313|EMBL:CCG18197.1};
RX PubMed=22541164; DOI=10.1016/j.vetmic.2012.03.041;
RA Hauser H., Richter D.C., van Tonder A., Clark L., Preston A.;
RT "Comparative genomic analyses of the Taylorellae.";
RL Vet. Microbiol. 159:195-203(2012).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome. {ECO:0000256|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00054}.
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DR EMBL; HE681423; CCG18197.1; -; Genomic_DNA.
DR RefSeq; WP_013521761.1; NC_021036.1.
DR AlphaFoldDB; I7IJA9; -.
DR GeneID; 79939779; -.
DR KEGG; teg:KUK_0897; -.
DR HOGENOM; CLU_002794_4_1_4; -.
DR OrthoDB; 9804431at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR CDD; cd01886; EF-G; 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 HAMAP; MF_00054_B; EF_G_EF_2_B; 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; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00054}; Hydrolase {ECO:0000313|EMBL:CCG18197.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00054}.
FT DOMAIN 8..290
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 701 AA; 77466 MW; 6BF39384A7CADB1D CRC64;
MARKTPINRY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
ITITSAATTA FWRGMGGNYP EHRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYCAVGGVQ
PQSETVWRQA NKYNVPRLAF VNKMDRTGAN FFKVYDQLKA RLNANPVPIV IPIGAEDTFS
GVVDLIKMKA IIWDEASQGT KFDYIDIPSE LEASAKEWRE KMVESAAESS EELMDKYLEE
GDLSEEDIIK ALRTRTIACE IQPMLCGTAF KNKGVQRMLD AVLDFLPSPV DIPPVQGEDA
DGNKAERKAD DKEKFSALAF KLMTDPFVGQ LTFIRVYSGV LNSGDTVLNS VKNKKERIGR
ILQMHANNRE EIKEVLAGDI AAVVGLKEVT TGETLCDVSS PIVLERMEFP EPVISQAVEP
KSKADQEKMG LALSRLAQED PSFRVRSDEE SGQTIISGMG ELHLEILVDR MKREFNVEAN
VGKPQVAYRE TIRKTVTDVE GKFVKQSGGR GQYGHVVLKL EPMEPGGEGY EFVDEIKGGV
VPREYIPAVD KGIQETLSSG VVAGYPVVDV KVTLTFGSYH DVDSNENAFR MAASMAFKEG
MRRASPVLLE PMMAVEVETP EDYAGTVMGD LSSRRGMVQG MDDMAGGGKS IKAEVPLAEM
FGYATNLRSL TQGRATYTME FKHYAEAPKN VAEEVISSRA K
//
