EFG_GLOVI
ID EFG_GLOVI Reviewed; 707 AA.
AC Q7NEF2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=glr3927;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC91868.1; -; Genomic_DNA.
DR RefSeq; NP_926873.1; NC_005125.1.
DR RefSeq; WP_011143915.1; NC_005125.1.
DR AlphaFoldDB; Q7NEF2; -.
DR SMR; Q7NEF2; -.
DR STRING; 251221.35214500; -.
DR PRIDE; Q7NEF2; -.
DR EnsemblBacteria; BAC91868; BAC91868; BAC91868.
DR KEGG; gvi:glr3927; -.
DR PATRIC; fig|251221.4.peg.3960; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_3; -.
DR InParanoid; Q7NEF2; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 88967at2; -.
DR PhylomeDB; Q7NEF2; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..707
FT /note="Elongation factor G"
FT /id="PRO_0000091129"
FT DOMAIN 8..297
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 96..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 150..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 707 AA; 77643 MW; 60E853E04200EDC3 CRC64;
MARNIPLERV RNIGIAAHID AGKTTTTERI LFYSGVIHKI GEVHEGNTVT DWMAQERERG
ITITAAAITT AWTRRDPENP TQPLPGALEH KINIIDTPGH VDFTIEVERS MRVLDGVITV
LCSVGGVQPQ TETVWRQANR YNVPRFIFVN KMDRTGANFY KVYSQVRDRL RANAVPIQLP
IGAEDTLSGI VDLVGMKAYV YGNDIGTDIR VEEIPADMEE LVQEYRAKLI EAVSETDDVL
LEKYFGGEEL TEAEIKAALR KGTVANTIVP MLCGSAFKNK GVQQMLDAVL DYLPSPLDIP
PIKGLLPNGT EVERSADDSQ PLSALAFKIM ADPYGRLTFV RVYSGILQKG SYALNASKDK
KERISRLIVL KADDRIEVDE LRAGDLGAVV GLKDTFTGDT LCTEDSPVIL ESLFIPEPVI
SVAIEPKTKA DLDKLSKALQ SLSEEDPTFR VHVDQETNQT IIAGMGELHL EILVDRMLRE
FKVEANVGAP QVAYRETIRK AVNNVEGLYK RQTGGKGQYG HVVINLEPGE PGTGFEFVSK
IVGGVVPKEY IGPAEQGMKE RCESGVIAGY PLIDVKVTMV DGSYHDVDSS EMAFKIAGSL
ALREAAQKAQ PVLLEPMMKV EVEVSGDFLG DVMGDLNARR GQIESMDNEG GVSKVTSRVP
LAEMFGYATD IRSKTQGRGT FSMEFSHYEE VPRNVAETII AKNKGNA
