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Database: UniProt/TrEMBL
Entry: A0A191ZIP5_9GAMM
LinkDB: A0A191ZIP5_9GAMM
Original site: A0A191ZIP5_9GAMM 
ID   A0A191ZIP5_9GAMM        Unreviewed;       397 AA.
AC   A0A191ZIP5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=A9404_10485 {ECO:0000313|EMBL:ANJ67742.1}, A9404_10550
GN   {ECO:0000313|EMBL:ANJ67754.1};
OS   Halothiobacillus sp. LS2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=1860122 {ECO:0000313|EMBL:ANJ67754.1, ECO:0000313|Proteomes:UP000078596};
RN   [1] {ECO:0000313|EMBL:ANJ67754.1, ECO:0000313|Proteomes:UP000078596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS2 {ECO:0000313|EMBL:ANJ67754.1,
RC   ECO:0000313|Proteomes:UP000078596};
RA   Luo J., Tan X., Lin W.;
RT   "Insight into the functional genes involving in sulfur oxidation in Pearl
RT   River water.";
RL   Submitted (JUN-2016) 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; CP016027; ANJ67742.1; -; Genomic_DNA.
DR   EMBL; CP016027; ANJ67754.1; -; Genomic_DNA.
DR   RefSeq; WP_066101216.1; NZ_CP016027.1.
DR   AlphaFoldDB; A0A191ZIP5; -.
DR   STRING; 1860122.A9404_10485; -.
DR   KEGG; haz:A9404_10485; -.
DR   KEGG; haz:A9404_10550; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000078596; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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:UP000078596}.
FT   DOMAIN          10..207
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   397 AA;  43098 MW;  BF45EA94B88F5E60 CRC64;
     MAKEKFERTK PHVNVGTIGH VDHGKTTLTA AITKVMAETF GGGSAMAFDQ IDKAPEEKAR
     GITISTSHVE YESATRHYAH VDCPGHADYV KNMITGAAQM DGAILVCSAA DGPMPQTREH
     ILLSRQVGVP YIVVFLNKAD MVDDPELLEL VEMEIRDLLS QYEFPGDDTP IITGSALKAL
     EGDQSEIGAP SVVRLVEAMD SYIPEPERAV DGTFLMPVED VFSISGRGTV VTGRVERGII
     KVGEEIEIVG IRDTQKTTVT GVEMFRKLLD QGQAGDNVGI LLRGTKRDDV ERGQVLCKPG
     SIKPHTKFEA EVYILSKDEG GRHTPFFNGY RPQFYFRTTD VTGSCVLPEG TEMVMPGDNV
     AMTVSLIAPI AMEDGLRFAI REGGRTVGAG VVSKIIE
//
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