(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHR2_GEOS0

ID   A0A0F6BHR2_GEOS0        Unreviewed;       692 AA.
AC   A0A0F6BHR2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 31.
DE   RecName: Full=Elongation factor G {ECO:0000256|HAMAP-Rule:MF_00054};
DE            Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN   OrderedLocusNames=GY4MC1_0107 {ECO:0000313|EMBL:ADP72963.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72963.1};
RN   [1] {ECO:0000313|EMBL:ADP72963.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72963.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome changes
CC       from the pre-translocational (PRE) to the post-translocational (POST)
CC       state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC       deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC       coordinated movement of the two tRNA molecules, the mRNA and
CC       conformational changes in the ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00054}.
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DR   EMBL; CP002293; ADP72963.1; -; Genomic_DNA.
DR   RefSeq; WP_003247555.1; NC_014650.1.
DR   EnsemblBacteria; ADP72963; ADP72963; GY4MC1_0107.
DR   GeneID; 29237257; -.
DR   KEGG; gmc:GY4MC1_0107; -.
DR   KO; K02355; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   BioCyc; GSP581103:G1GOQ-134-MONOMER; -.
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; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
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; 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;
DR   PRODOM; A0A0F6BHR2.
DR   SWISS-2DPAGE; A0A0F6BHR2.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00054,
KW   ECO:0000313|EMBL:ADP72963.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00054}.
FT   DOMAIN          8..282
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NP_BIND         17..24
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   NP_BIND         81..85
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   NP_BIND         135..138
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   COILED          204..224
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   692 AA;  77215 MW;  45EC52A85FD2981E CRC64;
     MAREFSLEKT RNIGIMAHID AGKTTTTERI LFYTGRVHKI GEVHEGAATM DWMEQEQERG
     ITITSAATTA QWKGHRINII DTPGHVDFTV EVERSLRVLD GAITVLDAQS GVEPQTETVW
     RQATTYGVPR IVFVNKMDKI GADFLYSVNT LHERLQANAH PVQLPIGAED QFSGIIDLVE
     MCAYHYHDEL GKNIERIEIP EEYRDMAEEY HNKLIEAVAE LDEELMMKYL EGEEITVEEL
     KAAIRRATIS VEFFPVFCGS AFKNKGVQLL LDGVVDYLPS PVDIPPIKGI VPDTEEEVVR
     ESSDDAPFAA LAFKIMTDPY VGKLTFFRVY SGTLDSGSYV MNSTKRKRER IGRLLQMHAN
     HRQEISTVYA GDIAAAVGLK DTTTGDTLCD EKNLVVLESM EFPEPVINVA IEPKSKADQD
     KMGQALQKLQ EEDPTFRAWT DPETGQTIIA GMGELHLDII VDRMRREFKV EANVGAPQVA
     YRETFRKSAQ VEGKFIRQSG GRGQYGHVWI EFSPNERGKG FEFENAIVGG VVPKEYVPAV
     QAGLEEAMQN GVLAGYPVVD IKAKLFDGSY HDVDSSEMAF KIAASLALKN AAEKCDPVLL
     EPIMKVEVII PEEYLGDIMG DITSRRGRVE GMEARGNAQV VRAMVPLAEM FGYATSLRSN
     TQGRGTFTMV FDHYEEVPKN IADEIIKKNK GE
//

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