ID A0A1A5X7F0_9BURK Unreviewed; 700 AA.
AC A0A1A5X7F0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=fusA {ECO:0000256|HAMAP-Rule:MF_00054,
GN ECO:0000313|EMBL:OBR48993.1};
GN ORFNames=A6456_21705 {ECO:0000313|EMBL:OBR48993.1}, C7399_12220
GN {ECO:0000313|EMBL:PZW74887.1};
OS Paraburkholderia tropica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=92647 {ECO:0000313|EMBL:OBR48993.1, ECO:0000313|Proteomes:UP000093802};
RN [1] {ECO:0000313|Proteomes:UP000093802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P-31 {ECO:0000313|Proteomes:UP000093802};
RA Kaur C., Selvakumar G., Ganeshamurthy A.N.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OBR48993.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P-31 {ECO:0000313|EMBL:OBR48993.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PZW74887.1, ECO:0000313|Proteomes:UP000248793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIr-6529 {ECO:0000313|EMBL:PZW74887.1,
RC ECO:0000313|Proteomes:UP000248793};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBR48993.1}.
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DR EMBL; LXGI01000094; OBR48993.1; -; Genomic_DNA.
DR EMBL; QKZC01000022; PZW74887.1; -; Genomic_DNA.
DR RefSeq; WP_065062799.1; NZ_QKZC01000022.1.
DR AlphaFoldDB; A0A1A5X7F0; -.
DR STRING; 92647.SAMN05216550_1442; -.
DR GeneID; 61303509; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000093802; Unassembled WGS sequence.
DR Proteomes; UP000248793; Unassembled WGS sequence.
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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000093802}.
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 700 AA; 77328 MW; 654AC9F50C3318C9 CRC64;
MARKTPIERY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
ITITSAATTA FWKGMGGNYP EHRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYCAVGGVQ
PQSETVWRQA NKYKVPRLAF VNKMDRTGAN FFKVYDQLKT RLKANPVPVV VPIGAEDTFQ
GVVDLIKMKA IIWDEASQGT KFDYVDIPAE LVDSCNEWRE KMIESAAEAS EELMEKYLGG
EELTEAEVVK AIRDRTIACE IQPMLCGTAF KNKGVQRMLD AVIDFLPSPV DIPPVTGELE
NGEKAERRAA DDEKFSALAF KIMTDPFVGQ LIFFRAYSGV VNSGDTVLNS TKGKKERLGR
ILQMHANNRE EIKEVRAGDI AAAVGLKEAT TGDTLCDPAN PIILERMIFP EPVISQAVEP
KTKADQEKMG LALNRLAQED PSFRVQTDEE SGQTIISGMG ELHLEILVDR MKREFNVEAT
VGKPQVAYRE TIRATAKDVE GKFVKQSGGR GQFGHAVITL EPNEQGKGYE FLDEIKGGVI
PREFIPAVDK GIQETLKAGV LAGFPVVDVK VHLTFGSYHD VDSNENAFRM AGSMAFKEAM
RKAQPVILEP MMAVEVETPE DYMGNVMGDL SGRRGIVQGM EDMVGGGKIV RAEVPLSEMF
GYSTSLRSLS QGRATYTMEF KHYAEAPRNV ADAIISAKAK
//
