EFG1_SYNY3
ID EFG1_SYNY3 Reviewed; 695 AA.
AC P28371; P74556;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Elongation factor G 1;
DE Short=EF-G 1;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=slr1463;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8061323; DOI=10.1007/bf00029610;
RA Welsch P.L., Johnson D., Zhang Y., Breitenberger C.A.;
RT "Synechocystis sp. PCC6803 fusB gene, located outside of the str operon,
RT encodes a polypeptide related to protein synthesis factor EF-G.";
RL Plant Mol. Biol. 25:735-738(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P28371; P52231: trxA; NbExp=2; IntAct=EBI-862177, EBI-862916;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; X65159; CAA46277.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18663.1; -; Genomic_DNA.
DR PIR; S76751; S76751.
DR AlphaFoldDB; P28371; -.
DR SMR; P28371; -.
DR IntAct; P28371; 3.
DR STRING; 1148.1653752; -.
DR PaxDb; P28371; -.
DR EnsemblBacteria; BAA18663; BAA18663; BAA18663.
DR KEGG; syn:slr1463; -.
DR eggNOG; COG0480; Bacteria.
DR InParanoid; P28371; -.
DR OMA; FRVVQMM; -.
DR PhylomeDB; P28371; -.
DR Proteomes; UP000001425; 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 GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..695
FT /note="Elongation factor G 1"
FT /id="PRO_0000091243"
FT DOMAIN 6..281
FT /note="tr-type G"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 79..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 42
FT /note="H -> R (in Ref. 1; CAA46277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 76750 MW; 8727830BF9073223 CRC64;
MEKDLTRYRN IGIFAHVDAG KTTTTERILK LTGRIHKLGE VHEGESTMDF MEQEAERGIT
IQSAATSCFW KDHQLNVIDT PGHVDFTIEV YRSLKVLDGG IGVFCGSGGV EPQSETNWRY
ANDSKVARLI YINKLDRTGA DFYRVVKQVE TVLGAKPLVM TLPIGTENDF VGVVDILTEK
AYIWDDSGDP EKYEITDIPA DMVDDVATYR EMLIETAVEQ DDDLMEKYLE GEEISIDDIK
RCIRTGTRKL DFFPTYGGSS FKNKGVQLVL DAVVDYLPNP KEVPPQPEVD LEGEETGNYA
IVDPEAPLRA LAFKIMDDRF GALTFTRIYS GTLSKGDTIL NTATGKTERI GRLVEMHADS
REEIESAQAG DIVAIVGMKN VQTGHTLCDP KNPATLEPMV FPDPVISIAI KPKKKGMDEK
LGMALSKMVQ EDPSFQVETD EESGETIIKG MGELHLDIKM DILKRTHGVE VEMGKPQVAY
RESITQQVSD TYVHKKQSGG SGQYAKIDYI VEPGEPGSGF QFESKVTGGN VPREYWPAVQ
KGFDQSVVKG VLAGYPVVDL KVTLTDGGFH PVDSSAIAFE IAAKAGYRQS LPKAKPQILE
PIMAVDVFTP EDHMGDVIGD LNRRRGMIKS QETGPMGVRV KADVPLSEMF GYIGDLRTMT
SGRGQFSMVF DHYAPCPTNV AEEVIKEAKE RQAAA
