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Database: UniProt
Entry: EFG_LEPCP
LinkDB: EFG_LEPCP
Original site: EFG_LEPCP 
ID   EFG_LEPCP               Reviewed;         700 AA.
AC   B1Y7G9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   10-OCT-2018, entry version 70.
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};
GN   OrderedLocusNames=Lcho_3863;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001013; ACB36117.1; -; Genomic_DNA.
DR   RefSeq; WP_012348864.1; NC_010524.1.
DR   ProteinModelPortal; B1Y7G9; -.
DR   SMR; B1Y7G9; -.
DR   STRING; 395495.Lcho_3863; -.
DR   PRIDE; B1Y7G9; -.
DR   EnsemblBacteria; ACB36117; ACB36117; Lcho_3863.
DR   KEGG; lch:Lcho_3863; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; QGMDDMV; -.
DR   OrthoDB; POG091H02CO; -.
DR   BioCyc; LCHO395495:G1GBL-3891-MONOMER; -.
DR   Proteomes; UP000001693; 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; -; 2.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
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; TF_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; 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    700       Elongation factor G.
FT                                /FTId=PRO_1000091728.
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   700 AA;  77183 MW;  E59C712838AE6631 CRC64;
     MARQTPIERY RNIGISAHID AGKTTTTERI LYYTGVNHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTC FWKGMDRSLP EHRFNIIDTP GHVDFTIEVE RSMRVLDGAC MVYCAVGGVQ
     PQSETVWRQA NKYKVPRLAF VNKMDRTGAN FFKVVDQMKT RLRANPVPVV VPIGAEDSFT
     GVVDLLKMKA IIWDEASQGM KFSYEDIPAG LEGVAQEWRE KMVEAAAEAS EELMNKYLET
     GDLTEDEIKL ALRTRTIACE IQPMLCGTAF KNKGVQRMLD AVIDYLPSPV DIPPVTGTDD
     DDQPISRRAD DKEKFSALAF KLMTDPFVGQ LTFVRVYSGV LQSGSSVYNP IRGKKERIGR
     ILQMHANQRE EIKEILAGDI AACVGLKEVT TGETLCDIDS PITLVKMIFP EPVISQAVEP
     KTKADQEKMG IALGRLAAED PSFRVRTDEE SGQTIISGMG ELHLEIIVDR MKREFGVEAN
     VGKPQVAYRE TIRDLVKDVE GKFVRQSGGK GQYGHVVLTV EPQEPGAGFQ FVDAIKGGVV
     PREFIPAVEK GLIDTLPNGV LAGFPVVDVK VTLTFGSYHE VDSNENAFKM AASMGFKDGM
     RKAKPVILEP MMAVEVETPE DYAGTVMGDL SSRRGMVQGM DDMVGGGKVI KAEVPLSEMF
     GYSTSLRSAT QGRATYTMEF KHYSEAPKNV ADAIITARGK
//
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