EFTU_COXBU
ID EFTU_COXBU Reviewed; 397 AA.
AC Q83ES6; B5QS64; Q83ET7; Q9X6G1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tuf-1;
GN OrderedLocusNames=CBU_0221.2; ORFNames=CBU_0221b;
GN and
GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tuf-2;
GN OrderedLocusNames=CBU_0236;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-358, AND DEVELOPMENTAL STAGE.
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=10531263; DOI=10.1128/iai.67.11.6026-6033.1999;
RA Seshadri R., Hendrix L.R., Samuel J.E.;
RT "Differential expression of translational elements by life cycle variants
RT of Coxiella burnetii.";
RL Infect. Immun. 67:6026-6033(1999).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Nine Mile Crazy / RSA 514;
RX PubMed=17088354; DOI=10.1128/iai.00883-06;
RA Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J.,
RA Samuel J.E., Heinzen R.A.;
RT "Proteome and antigen profiling of Coxiella burnetii developmental forms.";
RL Infect. Immun. 75:290-298(2007).
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. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Found in the large cell variant (LCV) stage,
CC undetectable in the small cell variant (SCV) stage; at protein level.
CC LCVs are more metabolically active than SCVs.
CC {ECO:0000269|PubMed:10531263, ECO:0000269|PubMed:17088354}.
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; AE016828; ACI15245.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO89794.1; -; Genomic_DNA.
DR EMBL; AF136604; AAD32649.1; -; Genomic_DNA.
DR RefSeq; NP_819280.1; NC_002971.3.
DR RefSeq; WP_005771609.1; NC_002971.4.
DR RefSeq; YP_002332954.1; NC_002971.3.
DR AlphaFoldDB; Q83ES6; -.
DR SMR; Q83ES6; -.
DR STRING; 227377.CBU_0221b; -.
DR EnsemblBacteria; AAO89794; AAO89794; CBU_0236.
DR EnsemblBacteria; ACI15245; ACI15245; CBU_0221b.
DR GeneID; 1208103; -.
DR GeneID; 1208117; -.
DR KEGG; cbu:CBU_0221b; -.
DR KEGG; cbu:CBU_0236; -.
DR PATRIC; fig|227377.7.peg.217; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_6; -.
DR OMA; EGDKEWG; -.
DR Proteomes; UP000002671; 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 Protein biosynthesis; Reference proteome.
FT CHAIN 1..397
FT /note="Elongation factor Tu"
FT /id="PRO_1000015645"
FT DOMAIN 10..206
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 174..176
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 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 397 AA; 43526 MW; 8157B2CD749064FF CRC64;
MSKEKFVREK PHVNVGTIGH VDHGKTTLTA ALTKVLSEKY GGEKKAFDQI DNAPEERARG
ITIATSHVEY QSDKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
VLAKQVGVPN IVVYLNKADM VDDKELLELV EMEVRDLLNS YDFPGDETPI IVGSALKALE
GDKSEVGEPS IIKLVETMDT YFPQPERAID KPFLMPIEDV FSISGRGTVV TGRVERGIIK
VGDEIEIVGI KDTTKTTCTG VEMFRKLLDE GQAGDNVGIL LRGTKREEVE RGQVLAKPGS
ITPHKKFEAE IYVLSKEEGG RHTPFLQGYR PQFYFRTTDV TGQLLSLPEG IEMVMPGDNV
KVTVELIAPV AMDEGLRFAV REGGRTVGAG VVTKIIE
