(data stored in SCRATCH zone)

SWISSPROT: D4YYM6_SPHJU

ID   D4YYM6_SPHJU            Unreviewed;       690 AA.
AC   D4YYM6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 46.
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   ECO:0000313|EMBL:BAI95458.1};
GN   OrderedLocusNames=SJA_C1-06240 {ECO:0000313|EMBL:BAI95458.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95458.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95458.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:0000256|HAMAP-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; AP010803; BAI95458.1; -; Genomic_DNA.
DR   RefSeq; WP_007686589.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06240; -.
DR   EnsemblBacteria; BAI95458; BAI95458; SJA_C1-06240.
DR   GeneID; 29272297; -.
DR   KEGG; sjp:SJA_C1-06240; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; ISRIYQM; -.
DR   OrthoDB; POG091H02CO; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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; 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.
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;
DR   PRODOM; D4YYM6.
DR   SWISS-2DPAGE; D4YYM6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00054,
KW   ECO:0000313|EMBL:BAI95458.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        8    283       Tr-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      17     24       GTP. {ECO:0000256|HAMAP-Rule:MF_00054}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00054}.
FT   NP_BIND     135    138       GTP. {ECO:0000256|HAMAP-Rule:MF_00054}.
SQ   SEQUENCE   690 AA;  76476 MW;  DAFEC04E891F8E46 CRC64;
     MARSHPLERY RNFGIMAHID AGKTTTTERI LYYTGKSYKI GEVHDGAATM DWMEQEQERG
     ITITSAATTC FWNDHRLNII DTPGHVDFTI EVERSLRVLD GAVAAFDGVA GVEPQSETVW
     RQADKYKVPR MCFINKLDRT GANFYYCVQT IIDRLGATPA VLYLPIGAES DFKGLVDLVE
     NRAIIWKDEN LGAEFSYEEI PADLADKAAE YREKLIELAV EQDDDAMEAY LEGNLPDVAT
     LKKLIRKGTL GHAFVPVLCG SAFKNKGVQP LLDAVVDYLP SPLDIPDVQG INPDTDEPDS
     RKTADDAPFS GLAFKIMNDP FVGSLTFLRV YSGTLTKGSY LNSVKDKKEK IGRMLLMHAN
     SREDIDTAYA GDIVALAGLK ETTTGDTLCA ERQPIILERM EFPEPVIELS VEPKTKADQE
     KMGIALNRLA AEDPSFRVST DHESGQTIIK GMGELHLEIL VDRMKREFKV EANVGAPQVA
     YREYLAKKVD IDYTHKKQSG GSGQFGRVKV TVIPGERGSG YQFFDEIKGG NIPREYIPSV
     EKGFRETAET GHLIGFPIID FEVHLTDGAY HDVDSSALAF EICARGAMRE AAAKSGIKLL
     EPIMKVEVVT PEEYLGDVIG DMNSRRGQIQ GTDSRGNAQV VEAMVPLANM FGYVNQLRSF
     TQGRANYSMI FSHYDEVPQN VADEVKAKMA
//

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