(data stored in ACNUC7421 zone)

SWISSPROT: EFG_ALCBS

ID   EFG_ALCBS               Reviewed;         699 AA.
AC   Q0VSL8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 89.
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}; OrderedLocusNames=ABO_0382;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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:0000255|HAMAP-
CC       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}.
DR   EMBL; AM286690; CAL15830.1; -; Genomic_DNA.
DR   RefSeq; WP_011587677.1; NC_008260.1.
DR   SMR; Q0VSL8; -.
DR   STRING; 393595.ABO_0382; -.
DR   PRIDE; Q0VSL8; -.
DR   EnsemblBacteria; CAL15830; CAL15830; ABO_0382.
DR   KEGG; abo:ABO_0382; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231585; -.
DR   KO; K02355; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   BioCyc; ABOR393595:ABO_RS01995-MONOMER; -.
DR   Proteomes; UP000008871; 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; Q0VSL8.
DR   SWISS-2DPAGE; Q0VSL8.
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..699
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000263420"
FT   DOMAIN          8..290
FT                   /note="tr-type G"
FT   NP_BIND         17..24
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   NP_BIND         88..92
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   NP_BIND         142..145
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   699 AA;  77313 MW;  910028DA3DB1B9A0 CRC64;
     MARKTPLNRY RNIGICAHVD AGKTTTTERI LFYTGVSHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTT FWQGMDQQYD QHRINIIDTP GHVDFTIEVE RSLRVLDGAV VVFCGSSGVE
     PQSETVWRQA NKYEVPRIVF VNKMDRAGAD FDSVCNQIRK RLGASVVPIQ YNIGAEDNFK
     GVVDLIRMKA IFWNEEDMGM TYEEKDIPDD IKDRCDELRE QMTEAAAEGS EELMEKYLEE
     GDLSNDEIKA GLRQQVLANE IVLGLCGSAF KNKGVQALLD AVIEFLPAPD EVKAIQGVLP
     DGETVEARKS SDDEPFSALA FKIATDPFVG SLTFIRVYSG VLNSGDSVLN SVREKKERVG
     RLLQMHANSR EEIKEVLAGD IAACVGMKDV TTGDTLCDLK NPIVLERMEF PEPVISVAVE
     PKSKADQEKM GLALGRLAQE DPSFRVKTDE ETGQTIISGM GELHLDILVD RMRREFKVEA
     NIGAPQVAYR ETFTRGADVD GKFVKQSGGR GQYGHVKVKF EPIDRDEEFQ FEEQIHGGSV
     PKEYFGAVQK GIDEQLQAGV LAGYPILGVK ATLYDGSYHE VDSNENAFRM AGALAVKNAA
     KEAGAVLLEP IMKVEAVTPE DYMGDVMGDL NRRRGIVQGM EDTMAGKIIR AEVPLSEMFG
     YATDLRSMSQ GRASYSMEFL KYAEAPKNIA DEVISGKKS
//

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