ID   D5H2S7_LACCS            Unreviewed;       396 AA.
AC   D5H2S7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tufA {ECO:0000313|EMBL:CBL50312.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=LCRIS_00865 {ECO:0000313|EMBL:CBL50312.1};
OS   Lactobacillus crispatus (strain ST1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL50312.1, ECO:0000313|Proteomes:UP000002371};
RN   [1] {ECO:0000313|EMBL:CBL50312.1, ECO:0000313|Proteomes:UP000002371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST1 {ECO:0000313|EMBL:CBL50312.1,
RC   ECO:0000313|Proteomes:UP000002371};
RX   PubMed=20435723; DOI=10.1128/JB.00399-10;
RA   Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA   Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.;
RT   "Genome sequence of Lactobacillus crispatus ST1.";
RL   J. Bacteriol. 192:3547-3548(2010).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
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DR   EMBL; FN692037; CBL50312.1; -; Genomic_DNA.
DR   RefSeq; WP_013086177.1; NC_014106.1.
DR   AlphaFoldDB; D5H2S7; -.
DR   GeneID; 69823280; -.
DR   KEGG; lcr:LCRIS_00865; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_1_9; -.
DR   Proteomes; UP000002371; 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   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   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   NCBIfam; TIGR00485; EF-Tu; 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 {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}.
FT   DOMAIN          11..205
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         137..140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   396 AA;  43604 MW;  97D73EC2AEE0376D CRC64;
     MAEKEHYVRT KPHVNIGTIG HVDHGKTTLT AAITTVLADK GLAKAEDYSQ IDAAPEEKER
     GITINTAHVE YETENRHYAH MDAPGHADYI KNMITGAAQM DGAILVVAAT DGPMPQTREH
     ILLARQVGVN YIVVFLNKCD LVDDPELIDL VEMEVRDLLT EYDYPGDDIP VVRGSALKAL
     QGDKEAQEQI LKLMDVVDEY IPTPERQTDK PFLMPVEDVF TITGRGTVAS GRIDRGTVKV
     GDEVEIVGLV DKVLKSVVTG LEMFHKTLDL GEAGDNVGVL LRGIDRDQVV RGQVLAAPGS
     IQTHKEFKGQ VYILKKEEGG RHTPFFSDYR PQFYFHTTDI TGEIELPEGT EMVMPGDNTE
     FTVKLIKPAA IEKGTKFTIR EGGRTVGAGQ VTEILD
//