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Database: UniProt/TrEMBL
Entry: A0A1D7QZX4_9BACI
LinkDB: A0A1D7QZX4_9BACI
Original site: A0A1D7QZX4_9BACI 
ID   A0A1D7QZX4_9BACI        Unreviewed;       396 AA.
AC   A0A1D7QZX4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=tuf {ECO:0000256|HAMAP-Rule:MF_00118,
GN   ECO:0000313|EMBL:AOM84563.1};
GN   ORFNames=BBEV_3248 {ECO:0000313|EMBL:AOM84563.1};
OS   Salisediminibacterium beveridgei.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Salisediminibacterium.
OX   NCBI_TaxID=632773 {ECO:0000313|EMBL:AOM84563.1, ECO:0000313|Proteomes:UP000094463};
RN   [1] {ECO:0000313|EMBL:AOM84563.1, ECO:0000313|Proteomes:UP000094463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLTeJB {ECO:0000313|EMBL:AOM84563.1,
RC   ECO:0000313|Proteomes:UP000094463};
RA   Hanson T.E., Mesa C., Basesman S.M., Oremland R.S.;
RT   "The complete genome sequence of Bacillus beveridgei MLTeJB.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012502; AOM84563.1; -; Genomic_DNA.
DR   RefSeq; WP_069366434.1; NZ_CP012502.1.
DR   AlphaFoldDB; A0A1D7QZX4; -.
DR   STRING; 632773.BBEV_3248; -.
DR   KEGG; bbev:BBEV_3248; -.
DR   PATRIC; fig|632773.3.peg.3410; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000094463; 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}; Reference proteome {ECO:0000313|Proteomes:UP000094463}.
FT   DOMAIN          10..205
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..26
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;  43332 MW;  1A4570D4D8608582 CRC64;
     MGKAKFDRSK THANIGTIGH VDHGKTTLTA AISSVLHKKS GKGTAMAYDQ IDGAPEERER
     GITISTAHVE YETDTRHYAH VDCPGHADYV KNMITGAAQM DGAILVVSAA DGPMPQTREH
     ILLSRQVGVP YIVVFLNKVD MVDDEELLEL VEMEVRDLLS EYDFPGDDIP VIAGSALKAL
     EGDEEYSQKI FELMEAVDTY IPTPERDKDK PFMMPVEDVF SITGRGTVAT GRVERGQLNV
     GDEVDIIGLE DETKKTTVTG VEMFRKLLDY AEAGDNIGAL LRGVSRDDIN RGQVLAKPGT
     ITPHTKFQAE VYVLSKDEGG RHTPFFTNYR PQFYFRTTDV TGIIHLPSGV EMVMPGDNVE
     MTVELIAPIA IEEGTKFSIR EGGRTVGAGV VASITE
//
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