(data stored in ACNUC7421 zone)

SWISSPROT: EFG_BACSU

ID   EFG_BACSU               Reviewed;         692 AA.
AC   P80868; P70980;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   11-DEC-2019, entry version 146.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
DE   AltName: Full=Vegetative protein 19;
DE            Short=VEG19;
GN   Name=fusA; Synonyms=fus; OrderedLocusNames=BSU01120;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA   Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA   Kawamura F., Yoshikawa H., Takahashi H.;
RT   "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT   subtilis chromosome.";
RL   Microbiology 142:3039-3046(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 235 AND 675.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [5]
RP   PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=12399479; DOI=10.1128/jb.184.22.6109-6114.2002;
RA   Gaidenko T.A., Kim T.-J., Price C.W.;
RT   "The PrpC serine-threonine phosphatase and PrkC kinase have opposing
RT   physiological roles in stationary-phase Bacillus subtilis cells.";
RL   J. Bacteriol. 184:6109-6114(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-302; SER-569 AND
RP   SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated on threonine residue(s). Phosphorylated by PrkC and
CC       dephosphorylated by PrpC, in vitro. {ECO:0000269|PubMed:12399479,
CC       ECO:0000269|PubMed:17218307}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000305}.
DR   EMBL; D64127; BAA11003.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11888.2; -; Genomic_DNA.
DR   PIR; B69628; B69628.
DR   RefSeq; NP_387993.2; NC_000964.3.
DR   RefSeq; WP_003235056.1; NZ_JNCM01000029.1.
DR   PDB; 5VH6; X-ray; 2.61 A; A=1-406.
DR   PDBsum; 5VH6; -.
DR   SMR; P80868; -.
DR   IntAct; P80868; 4.
DR   MINT; P80868; -.
DR   STRING; 224308.BSU01120; -.
DR   iPTMnet; P80868; -.
DR   jPOST; P80868; -.
DR   PaxDb; P80868; -.
DR   PRIDE; P80868; -.
DR   EnsemblBacteria; CAB11888; CAB11888; BSU01120.
DR   GeneID; 936826; -.
DR   KEGG; bsu:BSU01120; -.
DR   PATRIC; fig|224308.179.peg.115; -.
DR   eggNOG; ENOG4105CEJ; Bacteria.
DR   eggNOG; COG0480; LUCA.
DR   HOGENOM; HOG000231587; -.
DR   InParanoid; P80868; -.
DR   KO; K02355; -.
DR   OMA; AATTCHW; -.
DR   PhylomeDB; P80868; -.
DR   BioCyc; BSUB:BSU01120-MONOMER; -.
DR   Proteomes; UP000001570; 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; IBA:GO_Central.
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   1: Evidence at protein level;
DR   PRODOM; P80868.
DR   SWISS-2DPAGE; P80868.
KW   3D-structure; Cytoplasm; Direct protein sequencing; Elongation factor;
KW   GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298659"
FT   CHAIN           2..692
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091071"
FT   DOMAIN          8..282
FT                   /note="tr-type G"
FT   NP_BIND         17..24
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         81..85
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         135..138
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         569
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   CONFLICT        235
FT                   /note="I -> L (in Ref. 1; BAA11003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        675
FT                   /note="E -> G (in Ref. 1; BAA11003)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..16
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   TURN            19..22
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           23..33
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          66..72
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          75..80
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           90..98
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          100..107
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   TURN            108..110
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           114..125
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          130..135
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          137..139
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           144..153
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          159..166
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           169..171
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          174..177
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   TURN            178..181
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          182..185
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          188..191
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           201..203
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           204..219
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           223..230
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           237..249
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          254..258
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   TURN            261..264
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           267..277
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   HELIX           281..283
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          287..290
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          297..300
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          304..306
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          309..316
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   TURN            319..321
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          324..332
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          338..342
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   TURN            343..346
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          347..351
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          353..357
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          362..368
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          373..378
FT                   /evidence="ECO:0000244|PDB:5VH6"
FT   STRAND          387..389
FT                   /evidence="ECO:0000244|PDB:5VH6"
SQ   SEQUENCE   692 AA;  76617 MW;  DF63375070008FC1 CRC64;
     MAREFSLEKT RNIGIMAHID AGKTTTTERI LFYTGRIHKI GETHEGASQM DWMEQEQERG
     ITITSAATTA QWKGYRVNII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW
     RQATTYGVPR IVFVNKMDKI GADFLYSVGT LRDRLQANAH AIQLPIGAED NFEGIIDLVE
     NVAYFYEDDL GTRSDAKEIP EEYKEQAEEL RNSLIEAVCE LDEELMDKYL EGEEITIDEL
     KAGIRKGTLN VEFYPVLVGS AFKNKGVQLV LDAVLDYLPA PTDVAAIKGT RPDTNEEIER
     HSSDEEPFSA LAFKVMTDPY VGKLTFFRVY SGTLDSGSYV KNSTKGKRER VGRILQMHAN
     SREEISTVYA GDIAAAVGLK DTTTGDTLCD EKDLVILESM EFPEPVIDVA IEPKSKADQD
     KMGIALAKLA EEDPTFRTQT NPETGQTIIS GMGELHLDII VDRMKREFKV EANVGAPQVA
     YRETFRTGAK VEGKFVRQSG GRGQFGHVWI EFEPNEEGAG FEFENAIVGG VVPREYIPAV
     QAGLEDALEN GVLAGFPLID IKAKLFDGSY HDVDSNEMAF KVAASMALKN AVSKCNPVLL
     EPIMKVEVVI PEEYMGDIMG DITSRRGRVE GMEARGNAQV VRAMVPLAEM FGYATALRSN
     TQGRGTFTMH MDHYEEVPKS VAEEIIKKNK GE
//

If you have problems or comments...

PBIL Back to PBIL home page