EFG_XANP2
ID EFG_XANP2 Reviewed; 691 AA.
AC A7IFX8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=Xaut_1676;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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; CP000781; ABS66921.1; -; Genomic_DNA.
DR RefSeq; WP_012113699.1; NC_009720.1.
DR AlphaFoldDB; A7IFX8; -.
DR SMR; A7IFX8; -.
DR STRING; 78245.Xaut_1676; -.
DR PRIDE; A7IFX8; -.
DR EnsemblBacteria; ABS66921; ABS66921; Xaut_1676.
DR KEGG; xau:Xaut_1676; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_5; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 88967at2; -.
DR PhylomeDB; A7IFX8; -.
DR Proteomes; UP000002417; 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; cd01434; EFG_mtEFG1_IV; 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"
FT /id="PRO_1000091781"
FT DOMAIN 8..283
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 691 AA; 75965 MW; B5DB48758DC6AF7F CRC64;
MPRTHAIEDY RNFGIMAHID AGKTTTTERI LYYTGKSHKI GEVHDGAATM DWMTQEQERG
ITITSAATTA IWAGKRLNII DTPGHVDFTI EVERSLRVLD GAVCVLDGNQ GVEPQTETVW
RQADKYNVPR IVFVNKMDKI GADFYRCVEM IVDRVAGNPV CCQLPIGSEN NFKGVIDLVR
MKAVVWEDEA LGAKYHDEEI PADLADKAAE YRNKLVEAAV ELDDDAMTAY LDGVEPDVAT
LKSLIRKAVI GRKFNPVFCG SAFKNKGVQP LLDAVVDFLP SPIDRGAIKG IDFKTEEDTV
RMPSDDEPTS VLAFKIMDDP FVGTITFCRV YAGKMETGMG LLNSTRDKRE RVGRMLLMHA
NNREDIKEAY AGDIVALAGL KDVRTGDTLC DPAKAVILEK MEFPEPVIEI AIEPKSKADQ
EKLGIALSKL AAEDPSFRVS TDFESGQTIL KGMGELHLDI KVDILKRTYK VDANIGAPQV
AYRETITKKY EVDYTHKKQT GGTGQFARVK FIVEPNEVGK GFVFESAIVG GAVPKEYIPG
VQKGLESVLG AGVLAGFPVV DVKVQLIDGA FHEVDSSALA FEIASRAAFR EALQKGSPVL
LEPIMKVEVV TPEDYTGSVI GDLNSRRGQI QGQDMRGNAN VVNAMVPLAN MFGYVNTLRS
FSQGRATFTM QFDHYEQVPS NVAQEVQAKY A
