EFG1_PSET1
ID EFG1_PSET1 Reviewed; 704 AA.
AC Q3ILP5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=PSHAa0226;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85329.1; -; Genomic_DNA.
DR RefSeq; WP_011326943.1; NC_007481.1.
DR AlphaFoldDB; Q3ILP5; -.
DR SMR; Q3ILP5; -.
DR STRING; 326442.PSHAa0226; -.
DR EnsemblBacteria; CAI85329; CAI85329; PSHAa0226.
DR KEGG; pha:PSHAa0226; -.
DR PATRIC; fig|326442.8.peg.217; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_6; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 88967at2; -.
DR BioCyc; PHAL326442:PSHA_RS01115-MON; -.
DR Proteomes; UP000006843; Chromosome I.
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..704
FT /note="Elongation factor G 1"
FT /id="PRO_0000225227"
FT DOMAIN 8..290
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 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 704 AA; 77485 MW; 0114DB8520747784 CRC64;
MARTTPLERY RNIGICAHVD AGKTTTTERI LFYTGLSHKI GETHDGAATM DWMEQEQERG
ITITSAATTC FWKGMDAQFD AHRINIIDTP GHVDFTIEVE RSLRVLDGAV VVLCASSGVQ
PQTETVWRQA NKYEVPRMIF VNKMDRTGAD FFAVVDQVKS RLGATPVPIQ LPIGAEDGFK
GVIDLIKMKA INWNEADQGM TFTYEAIPAE LQELADEWRS HLVESAAEAT EELMDKYLEG
EELSEAEIKE ALRQRTLAND IVPMTCGSAF KNKGVQAVLD CVVEYMPAPT QVKQIQGILE
DGTEEERPAD DKAPFAALAF KIATDPFVGT LTFFRVYSGT VKQGDAVYNP VKSKRERLGR
IVQMHSNSRE EIKEVFAGDI AAAIGLKDVT TGETLCDPKS IITLERMEFP EPVISVAVEP
RTIADQDKMG IALGKLAAED PSFRVQTDEE SGQIIISGMG ELHLDILVER MKREFSVECN
VGKPQVAYRE AIRSTVKVEG KFIRQSGGRG QYGHVWLKLE PMDITDDEAP IYEFVNETVG
GSIPKEYVPA VDKGIQEQMS QGVLAGYPLL GVKATLYDGS FHDVDSNEMA FKIAGSLAMK
QGALQASPVL LEPVMKVEVL TPEANMGDVV GDLNRRRGMI EGMEDALGGL KQINAQVPLS
EMFGYATDLR SATQGRASYS MEFLKYAEAS KHVAETIISA RAVI
