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Database: UniProt
Entry: Q93QB0_STRMT
LinkDB: Q93QB0_STRMT
Original site: Q93QB0_STRMT 
ID   Q93QB0_STRMT            Unreviewed;       269 AA.
AC   Q93QB0;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   03-MAY-2023, entry version 79.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554};
DE   Flags: Fragment;
GN   Name=tuf {ECO:0000313|EMBL:AAK69066.1};
OS   Streptococcus mitis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=28037 {ECO:0000313|EMBL:AAK69066.1};
RN   [1] {ECO:0000313|EMBL:AAK69066.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 49456 {ECO:0000313|EMBL:AAK69066.1};
RX   PubMed=15297518; DOI=10.1128/JCM.42.8.3686-3695.2004;
RA   Picard F.J., Ke D., Boudreau D.K., Boissinot M., Huletsky A., Richard D.,
RA   Ouellette M., Roy P.H., Bergeron M.G.;
RT   "Use of tuf sequences for genus-specific PCR detection and phylogenetic
RT   analysis of 28 streptococcal species.";
RL   J. Clin. Microbiol. 42:3686-3695(2004).
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR   EMBL; AF276269; AAK69066.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93QB0; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR027417; P-loop_NTPase.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
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   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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000313|EMBL:AAK69066.1}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          1..102
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAK69066.1"
FT   NON_TER         269
FT                   /evidence="ECO:0000313|EMBL:AAK69066.1"
SQ   SEQUENCE   269 AA;  30014 MW;  9FB35F3ECEFC26A5 CRC64;
     ILVVASTDGP MPQTREHILL SRQVGVKHLI VFMNKVDLVD DEELLELVEM EIRDLLSEYD
     FPGDDLPVIQ GSALKALEGD TKYEDIVMEL MNTVDEYIPE PERDTDKPLL LPVEDVFSIT
     GRGTVASGRI DRGIVKVNDE IEIVGIKEET QKAVVTGVEM FRKQLDEGLA GDNVGVLLRG
     VQRDEIERGQ VIAKPGSINP HTKFKGEVYI LTKEEGGRHT PFFNNYRPQF YFRTTDVTGS
     IELPAGTEMV MPGDNVTIDV ELIHPIAVE
//
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