ID X4R9F3_9ACTO Unreviewed; 706 AA.
AC X4R9F3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Elongation factor G {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:SUO86826.1};
GN ORFNames=B1R42_05260 {ECO:0000313|EMBL:OQD37968.1}, NCTC5224_00487
GN {ECO:0000313|EMBL:SUO86826.1};
OS Trueperella pyogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=1661 {ECO:0000313|EMBL:SUO86826.1, ECO:0000313|Proteomes:UP000254485};
RN [1] {ECO:0000313|EMBL:OQD37968.1, ECO:0000313|Proteomes:UP000191477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFV1 {ECO:0000313|EMBL:OQD37968.1,
RC ECO:0000313|Proteomes:UP000191477};
RA Duarte V.S., Treu L., Campanaro S., Dias R.S., Da Silva C., Giacomini A.,
RA Corich V., De Paula S.O.;
RT "The complete genome sequence of Trueperella pyogenes UFV1 reveals an AI-2
RT transporter and processing system involved in quorum sensing signal-
RT response.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SUO86826.1, ECO:0000313|Proteomes:UP000254485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5224 {ECO:0000313|EMBL:SUO86826.1,
RC ECO:0000313|Proteomes:UP000254485};
RG Pathogen Informatics;
RA Doyle S.;
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|ARBA:ARBA00024731,
CC ECO:0000256|HAMAP-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; MVGS01000032; OQD37968.1; -; Genomic_DNA.
DR EMBL; UHHW01000002; SUO86826.1; -; Genomic_DNA.
DR AlphaFoldDB; X4R9F3; -.
DR Proteomes; UP000191477; Unassembled WGS sequence.
DR Proteomes; UP000254485; 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: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}.
FT DOMAIN 10..291
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 706 AA; 77931 MW; 30C785420FAF8381 CRC64;
MAHTPQKDLR KVRNIGIMAH IDAGKTTTTE RILFYTGLNY KMGETHDGAS TTDWMEQEKE
RGITITSAAV TTFWHNNQIN IIDTPGHVDF TVEVERSLRV LDGAVAVFDG KEGVEPQSET
VWRQADKYNV PRICFINKMD KMGADFDRAV QTIRDRLKAN PLILAFPIGA ESELSGVVDV
LNRKAIRFPA KDDKGNDTMG SLVVEEEIPA DLQDKADELY NELVETVAES DEALLDKYLG
GEEITIAELK AGIRKLTIAG ELYPIYAGSA YKNIGVQPVL DAVVDYLPSP QDVEFIEGMD
VKDEDVVVKR KPAPTEPFAA LAFKIAAHPF FGRLTYIRVY AGRIEPGDQI LNASKGKKER
VSKIFQMHSN KEQPVESASA GNIYAVIGLK DTTTGDSLSA LDAPMLLESM TFPDPVIHVA
VEPKSKADQE KLGLAIQKLA EEDPTFTVRL DEESGQTVIG GMGELHLDVL VDRMKREFKV
EANVGAPMVA YRETIRGKAE HIDYTHKKQT GGSGQFAKVI VTFEPLEENE EGKTYEFVDS
VTGGRVPREY IPSVDAGIQA AMENGVLAGF PMVNVKATLE DGAYHDVDSS EMAFKIAGQM
VFREGVKRAK PVILEPLMDV EVRTPEEYMG DVIGDLNSRR GQISSMEDAT GVKIVRALVP
LSEMFGYVGD LRSKTQGRAV YTMQFAKYQE VPKNVSDEII QKAHGE
//
