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   27-MAR-2024, entry version 158.
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; Bacillota; 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 the
RT   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 Bacillus
RT   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., 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   [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., Seror S.J.;
RT   "CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr
RT   kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.";
RL   Microbiology 155:932-943(2009).
RN   [5]
RP   INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX   PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA   Gaballa A., Su T.T., Helmann J.D.;
RT   "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT   (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL   Redox Biol. 42:101935-101935(2021).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with BrxC
CC       (PubMed:33722570). {ECO:0000250|UniProtKB:P0CE48,
CC       ECO:0000269|PubMed:33722570}.
CC   -!- INTERACTION:
CC       P33166; P39751: mbl; NbExp=3; IntAct=EBI-2122675, EBI-2122805;
CC       P33166; 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}.
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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   AlphaFoldDB; P33166; -.
DR   SMR; P33166; -.
DR   DIP; DIP-52428N; -.
DR   IntAct; P33166; 7.
DR   MINT; P33166; -.
DR   STRING; 224308.BSU01130; -.
DR   iPTMnet; P33166; -.
DR   jPOST; P33166; -.
DR   PaxDb; 224308-BSU01130; -.
DR   EnsemblBacteria; CAB11889; CAB11889; BSU_01130.
DR   GeneID; 935965; -.
DR   KEGG; bsu:BSU01130; -.
DR   PATRIC; fig|224308.179.peg.116; -.
DR   eggNOG; COG0050; Bacteria.
DR   InParanoid; P33166; -.
DR   OrthoDB; 9804504at2; -.
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; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
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; T_Tr_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   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..396
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091291"
FT   DOMAIN          10..205
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          61..65
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          82..85
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          137..140
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          175..177
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         137..140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   MOD_RES         385
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000305|PubMed:19246764"
FT   MUTAGEN         385
FT                   /note="T->V: Not phosphorylated by PrkC in vitro."
FT                   /evidence="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
//