ID   EFTU_FRUSA              Reviewed;         147 AA.
AC   Q2YEJ1; P83541;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Elongation factor Tu;
DE   Flags: Fragments;
GN   Name=tuf;
OS   Fructilactobacillus sanfranciscensis (Lactobacillus sanfranciscensis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Fructilactobacillus.
OX   NCBI_TaxID=1625;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-9; 57-69 AND 84-97, AND INDUCTION.
RC   STRAIN=ATCC 27651 / DSM 20451 / JCM 5668 / KCTC 3205 / NCIMB 702811 / NRRL
RC   B-3934 / L-12;
RX   PubMed=12112860;
RX   DOI=10.1002/1615-9861(200206)2:6<765::aid-prot765>3.0.co;2-v;
RA   Drews O., Weiss W., Reil G., Parlar H., Wait R., Goerg A.;
RT   "High pressure effects step-wise altered protein expression in
RT   Lactobacillus sanfranciscensis.";
RL   Proteomics 2:765-774(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-147, AND INDUCTION.
RC   STRAIN=ATCC 27651 / DSM 20451 / JCM 5668 / KCTC 3205 / NCIMB 702811 / NRRL
RC   B-3934 / L-12;
RX   PubMed=16044264; DOI=10.1007/s00203-005-0021-4;
RA   Pavlovic M., Hoermann S., Vogel R.F., Ehrmann M.A.;
RT   "Transcriptional response reveals translation machinery as target for high
RT   pressure in Lactobacillus sanfranciscensis.";
RL   Arch. Microbiol. 184:11-17(2005).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By elevated hydrostatic pressure.
CC       {ECO:0000269|PubMed:12112860, ECO:0000269|PubMed:16044264}.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC       Tu/EF-1A subfamily. {ECO:0000305}.
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DR   EMBL; AY912112; AAX93321.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2YEJ1; -.
DR   SMR; Q2YEJ1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd03697; EFTU_II; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
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   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           <1..>147
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000285982"
FT   CONFLICT        57..58
FT                   /note="LG -> VA (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94..97
FT                   /note="IGAL -> LVDQ (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         147
SQ   SEQUENCE   147 AA;  16400 MW;  946327065AB323F5 CRC64;
     DLLSEYGYDL MDTVDEYIPT PERDERKPFM MPIEDVFTIT GRGTVASGRI ERGVIKLGDE
     VEIVGLVEDV LKTTVTGIEM FRKTLDEGQA GDNIGALLRG VNREQVVRGQ VLAAPGSVQT
     HEKFSAEVYI MSKEEGGRHT PFFSNYR