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Database: UniProt
Entry: Q5QWB4
LinkDB: Q5QWB4
Original site: Q5QWB4 
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   29-OCT-2014, entry version 67.
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=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. {ECO:0000255|HAMAP-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}.
CC   -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding)
CC       domain. {ECO:0000305}.
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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; SGVQPQT; -.
DR   OrthoDB; EOG6X6RBF; -.
DR   BioCyc; ILOI283942:GI0U-352-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; 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; IPR009000; Transl_B-barrel.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_II; 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   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    707       Elongation factor G.
FT                                /FTId=PRO_0000091136.
FT   DOMAIN        8    290       tr-type G.
FT   NP_BIND      17     24       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
FT   NP_BIND      88     92       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
FT   NP_BIND     142    145       GTP. {ECO:0000255|HAMAP-Rule:MF_00054}.
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
//
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