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
//