EFG1_SYNC1
ID EFG1_SYNC1 Reviewed; 691 AA.
AC Q3A834;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA1 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=Pcar_0197;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) 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:0000255|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00054}.
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DR EMBL; CP000142; ABA87458.1; -; Genomic_DNA.
DR RefSeq; WP_011339858.1; NC_007498.2.
DR AlphaFoldDB; Q3A834; -.
DR SMR; Q3A834; -.
DR STRING; 338963.Pcar_0197; -.
DR EnsemblBacteria; ABA87458; ABA87458; Pcar_0197.
DR KEGG; pca:Pcar_0197; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_7; -.
DR OMA; NSARHHE; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000002534; Chromosome.
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; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..691
FT /note="Elongation factor G 1"
FT /id="PRO_0000225224"
FT DOMAIN 7..282
FT /note="tr-type G"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 80..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 691 AA; 76453 MW; C3FD9B67A5E94C2F CRC64;
MTCPDLKNLR NIGIISHIDA GKTTVSERVL FYTGESHRIG EVHDGNAVMD WMEQEQERGI
TITATTTCCH WRDVRINLID TPGHIDFTIE VERSLRVLDS AVVIFSAVEG VQAQTESVWR
QADRYAVPRI CLINKMDRIG ADYRRVLEQM RKRFTTRPVL MHLPLGIEGD FAGVIDVLEG
RCLTFSETDQ GATVETCDIP EERQSEVAAA REQIVEAAAD FDDAILADFL EGRPIKAART
RAALRRGVLT CRLCPVFLGS ALRNKGIQPL LDAVIDYLPS PLQAPPIAAS PPNHQDATAE
PALLPCDPQG PLCALAFKVL SDAGRKLTYL RVYSGSLRAG DEILNSTQGV AEKVARLFRM
HAHKRERVTE VQAGDIVAAV GLKHALTGDT LCRAEQPLRL EGLRIPEPVV SLAVEPRHID
DREKLPAALE KLLWEDPTFR VREDADTGQT ILTGMGQLHL EIITDRLHRE FGVEVRTGRP
QVVYRETVQN SARHHERFHR ETEGRIQSGE VTLEIAPSGR GKGLRIVLPE DENPLPARLR
EELKKCLHQS CAAGIRTGYP LTDVEITIIE APFEPGLTTE IGLLAAAQRG LSLAATQAGL
TLLEPVMALE LTVPTEHAGQ VIGSLQQKHG RIDGLETRSE SELIQARAPL SQLFDYMGEL
RSVTRGRGTF AMEFSHYDPA PDEIQTLYGL L
