ID EFG_IDILO Reviewed; 707 AA.
AC Q5QWB4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 01-MAY-2013, entry version 56.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; OrderedLocusNames=IL0349;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome
CC changes from the pre-translocational (PRE) to the post-
CC translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two
CC tRNA molecules, the mRNA and conformational changes in the
CC ribosome (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-G/EF-2 subfamily.
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DR EMBL; AE017340; AAV81192.1; -; Genomic_DNA.
DR RefSeq; YP_154741.1; NC_006512.1.
DR ProteinModelPortal; Q5QWB4; -.
DR SMR; Q5QWB4; 1-701.
DR STRING; 283942.IL0349; -.
DR PRIDE; Q5QWB4; -.
DR EnsemblBacteria; AAV81192; AAV81192; IL0349.
DR GeneID; 3174221; -.
DR KEGG; ilo:IL0349; -.
DR PATRIC; 22138719; VBIIdiLoi21852_0351.
DR eggNOG; COG0480; -.
DR HOGENOM; HOG000231585; -.
DR KO; K02355; -.
DR OMA; GEICAFV; -.
DR ProtClustDB; PRK00007; -.
DR BioCyc; ILOI283942:GI0U-392-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR HAMAP; MF_00054_B; EF-G_EF-2_B; 1; -.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR009022; EFG_III-V.
DR InterPro; IPR000640; EFG_V.
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; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR Pfam; PF00679; EFG_C; 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; SSF54980; EFG_III_V; 2.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR SUPFAM; SSF50447; Translat_factor; 1.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1 707 Elongation factor G.
FT /FTId=PRO_0000091136.
FT NP_BIND 17 24 GTP (By similarity).
FT NP_BIND 88 92 GTP (By similarity).
FT NP_BIND 142 145 GTP (By similarity).
SQ SEQUENCE 707 AA; 78015 MW; BD6D91047E3C3425 CRC64;
MARKTSIERY RNIGICAHVD AGKTTTTERV LFYTGLSHKI GEVHDGAATM DWMEQEQERG
ITITSAATTC FWQGMDKQFP EHRVNIIDTP GHVDFTIEVE RSLRVLDGAV VVLCASSGVQ
PQTETVWRQA NKYEVPRMVF VNKMDRAGAD FLSVVHQMKT RLAAQAVPMQ LPVGAEDNFR
GVVDLVKMKF INWSEEDMGT SFTYEDIPAD MVDECEKYHG ELVEAAAEAN EELMNKYLEE
GELTEAEIKQ GLRIRTLAND ICLVACGSAF KNKGVQAVLD AVIEYLPSPT EVKPITGILD
DESEGVRKSS DEEPFSALAF KIATDPFVGT LTFVRVYSGV LNQGDGVVNP VKNKKERVGR
MVQMHSNSRE EIKEVRAGDI AALIGLKDVT TGDTLCDPAH KITLERMEFP EPVISVAVEP
KTKADQEKMG IALGKLAAED PSFRVKTDEE SGQTIISGMG ELHLDIIVDR MKREFKVECN
VGQPQVAYRE AIRDAVEIEG KFVRQSGGRG QFGHVWLKLE PMTIEEDANG DDITYKFVNE
IVGGVVPKEY IPAVDKGIQE QMQQGVLAGY PVLGVKATLY DGSYHDVDSS EMAFKIAGSM
AFKKGALKAN PALLEPMMKV EVITPEESMG DVVGDLNRRR GLIEGMEEAP GGLKAVNAQV
PLSEMFGYAT DLRSQTQGRA SYSMEFLKYA EAPNNIAEKV MAERNAK
//
