EFG_SYNP6
ID EFG_SYNP6 Reviewed; 694 AA.
AC P18667;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=syc0655_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2499762; DOI=10.1007/bf00332226;
RA Meng B.-Y., Shinozaki K., Sugiura M.;
RT "Genes for the ribosomal proteins S12 and S7 and elongation factors EF-G
RT and EF-Tu of the cyanobacterium, Anacystis nidulans: structural homology
RT between 16S rRNA and S7 mRNA.";
RL Mol. Gen. Genet. 216:25-30(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17442; CAA35495.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD78845.1; -; Genomic_DNA.
DR PIR; S04429; S04429.
DR RefSeq; WP_011242967.1; NC_006576.1.
DR AlphaFoldDB; P18667; -.
DR SMR; P18667; -.
DR STRING; 269084.syc0655_d; -.
DR EnsemblBacteria; BAD78845; BAD78845; syc0655_d.
DR KEGG; syc:syc0655_d; -.
DR eggNOG; COG0480; Bacteria.
DR OMA; AATTCHW; -.
DR Proteomes; UP000001175; 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.
FT CHAIN 1..694
FT /note="Elongation factor G"
FT /id="PRO_0000091241"
FT DOMAIN 8..285
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 694 AA; 75910 MW; D1ADFC7D515C9BFF CRC64;
MARSVPLEKV RNIGIAAHID AGKTTTTERI LFYSGVVHKI GEVHDGNAVT DWMEQERERG
ITITAAAIST SWKDYRVNII DTPGHVDFTI EVERSMRVLD GVVAVFCSVG GVQPQSETVW
RQADRYSVPR IVFVNKMDRT GADFFKVYGQ IRDRVRANAV PIQIPIGAES DFQGIVDLVE
MKAHIYTNDL GTDILVTDIP AELQETAAEW RSKMVEAVAE TDEALLDKYF EDGDLSIEDI
KAGLRKGVLI QGNDRLVPML CGSAFKNKGV QLLLDAVVEL LPSPQDIPPI QGTLPDGEVA
LRPSSDEAPF SALAFKIMAD PYGRLTFVRV YSGILQKGSY VYNATKGKKE RVSRLIILKA
DDRIEVDELR AGDLGAVLGL KDTFTGDTLC DDQNPIILES LFIPEPVISV AVEPKTKNDM
EKLSKALQAL SEEDPTFRVS VDSETNQTVI AGMGELHLEI LVDRMLREYK VEANIGAPQV
AYRETVRKAV KAEGKFVRQS GGKGQYGHVV IELEPAEPGT GFEFVSKIVG GTVPKEYVGP
AEQGMKETCE SGVLAGYPLI DIKATLVDGS YHDVDSSEMA FKIAGSMAIK EAVRKADPVL
LEPVMKVEVE VPEDFLGSVM GNLISRRGQI EGQATTNGTA TVSAKVPLAE MFGYATDLRS
MTQGRGIFTM EFSQYEEVPR NVAETIIAKN KGNA
