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 03-AUG-2022, entry version 150.
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 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; P33166; -.
DR PRIDE; P33166; -.
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 OMA; EGDKEWG; -.
DR PhylomeDB; P33166; -.
DR BioCyc; BSUB:BSU01130-MON; -.
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 Gene3D; 3.40.50.300; -; 1.
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 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 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
