EFTU_RICPR
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 03-AUG-2022, entry version 126.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {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; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC 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: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {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; NP_221025.1; NC_000963.1.
DR RefSeq; WP_004596195.1; NC_000963.1.
DR AlphaFoldDB; P48865; -.
DR SMR; P48865; -.
DR STRING; 272947.RP661; -.
DR PRIDE; P48865; -.
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; EGDKEWG; -.
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:InterPro.
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 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; 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 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
