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 03-AUG-2022, entry version 157.
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 / NRRL NRS-744 / 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}.
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; 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 AlphaFoldDB; P80868; -.
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; BSU_01120.
DR GeneID; 936826; -.
DR KEGG; bsu:BSU01120; -.
DR PATRIC; fig|224308.179.peg.115; -.
DR eggNOG; COG0480; Bacteria.
DR InParanoid; P80868; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; P80868; -.
DR BioCyc; BSUB:BSU01120-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0032790; P:ribosome disassembly; 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 Gene3D; 3.40.50.300; -; 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; T_Tr_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_III; 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;
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 BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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:0007829|PDB:5VH6"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:5VH6"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5VH6"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5VH6"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:5VH6"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:5VH6"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:5VH6"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:5VH6"
FT STRAND 387..389
FT /evidence="ECO:0007829|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
