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Database: UniProt
Entry: A8AQM8
LinkDB: A8AQM8
Original site: A8AQM8 
ID   EFG_CITK8               Reviewed;         704 AA.
AC   A8AQM8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   29-OCT-2014, entry version 48.
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=CKO_04746;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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}.
CC   -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding)
CC       domain. {ECO:0000305}.
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DR   EMBL; CP000822; ABV15791.1; -; Genomic_DNA.
DR   RefSeq; YP_001456227.1; NC_009792.1.
DR   ProteinModelPortal; A8AQM8; -.
DR   SMR; A8AQM8; 5-700.
DR   STRING; 290338.CKO_04746; -.
DR   EnsemblBacteria; ABV15791; ABV15791; CKO_04746.
DR   GeneID; 5584578; -.
DR   KEGG; cko:CKO_04746; -.
DR   PATRIC; 20391627; VBICitKos71230_3961.
DR   eggNOG; COG0480; -.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; SGVQPQT; -.
DR   OrthoDB; EOG6X6RBF; -.
DR   BioCyc; CKOS290338:GJ8L-4728-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    704       Elongation factor G.
FT                                /FTId=PRO_1000008815.
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   704 AA;  77460 MW;  7CD25D0AC0E978C6 CRC64;
     MARTTPIARY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTA FWSGMAKQYE PHRVNIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ
     PQSETVWRQA NKYKVPRIAF VNKMDRMGAN FLKVVGQIKS RLGANPVPLQ LAIGAEEAFT
     GVVDLVKMKA INWNEADAGV TFTYEDIPAD MQELAEEWHQ NLIESAAEAS EELMEKYLGG
     EELTEEEIKK ALRQRVLSNE IILVTCGSAF KNKGVQAMLD AVIDYLPSPV DVPAINGILD
     DGKDTPAERH ASDDEPFSAL AFKIATDPFV GNLTFFRVYS GVVNSGDTVL NSVKSARERF
     GRIVQMHANK REEIKEVRAG DIAAAIGLKD VTTGDTLCDP DAPIILERME FPEPVISIAV
     EPKTKADQEK MGLALGRLAK EDPSFRVWTD EESNQTIIAG MGELHLDIIV DRMKREFNVE
     ANVGKPQVAY REAIRSKVTD IEGKHAKQSG GRGQYGHVVI DMYPLEPGSN PKGYEFINDI
     KGGVIPGEYI PAVDKGIQEQ LKAGPLAGYP VVDIGIRLHF GSYHDVDSSE LAFKLAASIA
     FKEGFKKAKP VLLEPIMKVE VETPEENTGD VIGDLSRRRG MLRGQESEVT GVKIHAEVPL
     SEMFGYATQL RSLTKGRASY TMEFLKYDDA PSNVAQAVIE ARGK
//
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