ID   EFTU_RICPR              Reviewed;         394 AA.
AC   P48865;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   04-NOV-2026, entry version 142.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            EC=3.6.5.3 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=RP661;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=8892818; DOI=10.1128/jb.178.21.6192-6199.1996;
RA   Syvaenen A.-C., Amiri H., Jamal A., Andersson S.G.E., Kurland C.G.;
RT   "A chimeric disposition of the elongation factor genes in Rickettsia
RT   prowazekii.";
RL   J. Bacteriol. 178:6192-6199(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- FUNCTION: GTP hydrolase that promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00118};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00118};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
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; Z54170; CAA90881.1; -; Genomic_DNA.
DR   EMBL; AJ235272; CAA15101.1; -; Genomic_DNA.
DR   PIR; C71672; C71672.
DR   RefSeq; WP_004596195.1; NC_000963.1.
DR   AlphaFoldDB; P48865; -.
DR   SMR; P48865; -.
DR   STRING; 272947.gene:17555738; -.
DR   EnsemblBacteria; CAA15101; CAA15101; CAA15101.
DR   GeneID; 57569786; -.
DR   KEGG; rpr:RP661; -.
DR   PATRIC; fig|272947.5.peg.683; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_5; -.
DR   OMA; AACIEYQ; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000002480; 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:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   FunFam; 2.40.30.10:FF:000001; Elongation factor Tu; 1.
DR   FunFam; 3.40.50.300:FF:000003; Elongation factor Tu; 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; IPR050055; EF-Tu_GTPase.
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.
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; NF000766; PRK00049.1; 1.
DR   NCBIfam; NF009372; PRK12735.1; 1.
DR   NCBIfam; NF009373; PRK12736.1; 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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..394
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091378"
FT   DOMAIN          10..204
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         26
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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"
FT   CONFLICT        198
FT                   /note="S -> T (in Ref. 1; CAA90881)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205..207
FT                   /note="RAT -> ELQ (in Ref. 1; CAA90881)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  42921 MW;  510FB2997E389BBF CRC64;
     MAKAKFERTK PHVNIGTIGH VDHGKTSLTA AITIILAKTG GAKATAYDQI DAAPEEKERG
     ITISTAHVEY ETQNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLAKQVGVPA MVVFLNKVDM VDDPDLLELV EMEVRELLSK YGFPGNEIPI IKGSALQALE
     GKPEGEKAIN ELMNAVDSYI PQPIRATDKP FLMPIEDVFS ISGRGTVVTG RVESGIIKVG
     EEIEIVGLKN TQKTTCTGVE MFRKLLDEGQ SGDNVGILLR GTKREEVERG QVLAKPGSIK
     PHDKFEAEVY VLSKEEGGRH TPFTNDYRPQ FYFRTTDVTG TIKLPSDKQM VMPGDNATFS
     VELIKPIAMQ EGLKFSIREG GRTVGAGIVT KINN
//