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 01-MAY-2013, entry version 37.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; 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 (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; 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; QEPGKGY; -.
DR ProtClustDB; PRK00007; -.
DR BioCyc; CKOS290338:GJ8L-4728-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 1 704 Elongation factor G.
FT /FTId=PRO_1000008815.
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 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
//
