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Database: UniProt/SWISS-PROT
Entry: EFTU_BACSU
LinkDB: EFTU_BACSU
Original site: EFTU_BACSU 
ID   EFTU_BACSU              Reviewed;         396 AA.
AC   P33166;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   16-JAN-2019, entry version 134.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE   AltName: Full=P-40;
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA;
GN   OrderedLocusNames=BSU01130;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2110445; DOI=10.1007/BF00249075;
RA   Ludwig W., Weizenegger M., Betzl D., Leidel E., Lenz T., Ludvigsen A.,
RA   Moellenhoff D., Wenzig P., Schleifer K.H.;
RT   "Complete nucleotide sequences of seven eubacterial genes coding for
RT   the elongation factor Tu: functional, structural and phylogenetic
RT   evaluations.";
RL   Arch. Microbiol. 153:241-247(1990).
RN   [2]
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
RT   Bacillus subtilis chromosome.";
RL   Microbiology 142:3039-3046(1996).
RN   [3]
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   [4]
RP   PHOSPHORYLATION AT THR-385, AND MUTAGENESIS OF THR-385.
RC   STRAIN=168;
RX   PubMed=19246764; DOI=10.1099/mic.0.022475-0;
RA   Absalon C., Obuchowski M., Madec E., Delattre D., Holland I.B.,
RA   Seror S.J.;
RT   "CpgA, EF-Tu and the stressosome protein YezB are substrates of the
RT   Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.";
RL   Microbiology 155:932-943(2009).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P39751:mbl; NbExp=3; IntAct=EBI-2122675, EBI-2122805;
CC       Q01465:mreB; NbExp=6; IntAct=EBI-2122675, EBI-6406749;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Phosphorylated on Thr-385 in vitro by PrkC in the presence of
CC       poly-L-lysine or myelin basic protein, dephosphorylated by PrpC.
CC       {ECO:0000269|PubMed:19246764}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.
DR   EMBL; D64127; BAA11004.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11889.1; -; Genomic_DNA.
DR   PIR; A60663; A60663.
DR   RefSeq; NP_387994.1; NC_000964.3.
DR   RefSeq; WP_003235058.1; NZ_JNCM01000029.1.
DR   ProteinModelPortal; P33166; -.
DR   SMR; P33166; -.
DR   DIP; DIP-52428N; -.
DR   IntAct; P33166; 7.
DR   MINT; P33166; -.
DR   STRING; 224308.Bsubs1_010100000585; -.
DR   iPTMnet; P33166; -.
DR   jPOST; P33166; -.
DR   PaxDb; P33166; -.
DR   PRIDE; P33166; -.
DR   EnsemblBacteria; CAB11889; CAB11889; BSU01130.
DR   GeneID; 935965; -.
DR   KEGG; bsu:BSU01130; -.
DR   PATRIC; fig|224308.179.peg.116; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   InParanoid; P33166; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   PhylomeDB; P33166; -.
DR   BioCyc; BSUB:BSU01130-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   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 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   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    396       Elongation factor Tu.
FT                                /FTId=PRO_0000091291.
FT   DOMAIN       10    205       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      82     86       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     137    140       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       61     65       G2. {ECO:0000250}.
FT   REGION       82     85       G3. {ECO:0000250}.
FT   REGION      137    140       G4. {ECO:0000250}.
FT   REGION      175    177       G5. {ECO:0000250}.
FT   MOD_RES     385    385       Phosphothreonine.
FT                                {ECO:0000305|PubMed:19246764}.
FT   MUTAGEN     385    385       T->V: Not phosphorylated by PrkC in
FT                                vitro. {ECO:0000269|PubMed:19246764}.
SQ   SEQUENCE   396 AA;  43593 MW;  BC096F47AAE6F72A CRC64;
     MAKEKFDRSK SHANIGTIGH VDHGKTTLTA AITTVLHKKS GKGTAMAYDQ IDGAPEERER
     GITISTAHVE YETETRHYAH VDCPGHADYV KNMITGAAQM DGAILVVSAA DGPMPQTREH
     ILLSKNVGVP YIVVFLNKCD MVDDEELLEL VEMEVRDLLS EYDFPGDDVP VVKGSALKAL
     EGDAEWEAKI FELMDAVDEY IPTPERDTEK PFMMPVEDVF SITGRGTVAT GRVERGQVKV
     GDEVEIIGLQ EENKKTTVTG VEMFRKLLDY AEAGDNIGAL LRGVSREEIQ RGQVLAKPGT
     ITPHSKFKAE VYVLSKEEGG RHTPFFSNYR PQFYFRTTDV TGIIHLPEGV EMVMPGDNTE
     MNVELISTIA IEEGTRFSIR EGGRTVGSGV VSTITE
//
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