(data stored in ACNUC7421 zone)

SWISSPROT: C8W3Y2_DESAS

ID   C8W3Y2_DESAS            Unreviewed;       691 AA.
AC   C8W3Y2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   10-APR-2019, entry version 65.
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=Dtox_0283 {ECO:0000313|EMBL:ACV61236.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61236.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61236.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001720; ACV61236.1; -; Genomic_DNA.
DR   RefSeq; WP_015755957.1; NC_013216.1.
DR   STRING; 485916.Dtox_0283; -.
DR   EnsemblBacteria; ACV61236; ACV61236; Dtox_0283.
DR   KEGG; dae:Dtox_0283; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; ISRIYQM; -.
DR   OrthoDB; 88967at2; -.
DR   BioCyc; DACE485916:G1GFV-298-MONOMER; -.
DR   Proteomes; UP000002217; 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; -; 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; C8W3Y2.
DR   SWISS-2DPAGE; C8W3Y2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00054,
KW   ECO:0000313|EMBL:ACV61236.1};
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:UP000002217}.
FT   DOMAIN        8    282       Tr-type G. {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   691 AA;  76788 MW;  793B60F47692CA00 CRC64;
     MARKYALENT RNIGIMAHID AGKTTTTERI LFYTGRVHKL GEVHDGAATM DWMVQEQERG
     ITITSAATTC EWRDHCINII DTPGHVDFTM EVERSLRVLD GAVAVFCSVG GVEPQSETVW
     RQADKYRVPR IAYINKMDRI GADFFRGLTM IKDRLSANPV AVQLPIGVEE NFRGIVDLIR
     NKAIIYLDDL GTHSEESEIP PEMMEIADLY REKLLEAVAE SDEELMMKYL EGQSLTPEEI
     KLGIRKAALA VKIIPVLCGS SFKNKGVQPL LDAIVDFLPA PTDIPAVYGV DPESGEEDNR
     TAGDEEPFSA LAFKIMADPY VGKLTFFRVY SGHLSSGSYV YNSTKNRRER IGRILRMHAN
     HREEISEVFA GDIVAAVGLK STTTGDTLCD EEHPIILESM EFPEPVIDVS IEPKTKADQE
     KMGLALQKLA EEDPTFRIST NDETGQTIIS GMGELHLEVI VDRLLREFKV AANVGRPQVA
     FKETITKTVK AEGRFVRQSG GRGQYGHCMI TLEPMPHGDG YEFVNKIIGG VIPKEYIPAI
     DSGIREAMTT GQLAGYPMVD IRATVYDGSF HDVDSSEIAF KIAGSMALKN GAQKAAPVLM
     EPIMKIEVVV MEEYMGDVIG DISSRRGRIE EMEPRSNMQV IHGYVPLAEM FGYATELRSR
     TQGRGTYTMQ FSHYETVPQN IAEGIIAKRR G
//

If you have problems or comments...

PBIL Back to PBIL home page