ID A0A0F7HNC0_9STAP Unreviewed; 395 AA.
AC A0A0F7HNC0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-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:AKG75078.1};
GN ORFNames=AAT16_13310 {ECO:0000313|EMBL:AKG75078.1}, SAMN05216235_0919
GN {ECO:0000313|EMBL:SFK65465.1};
OS Salinicoccus halodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX NCBI_TaxID=407035 {ECO:0000313|EMBL:AKG75078.1, ECO:0000313|Proteomes:UP000034029};
RN [1] {ECO:0000313|EMBL:AKG75078.1, ECO:0000313|Proteomes:UP000034029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3B36 {ECO:0000313|EMBL:AKG75078.1,
RC ECO:0000313|Proteomes:UP000034029};
RX PubMed=26634017;
RA Jiang K., Xue Y., Ma Y.;
RT "Complete genome sequence of Salinicoccus halodurans H3B36, isolated from
RT the Qaidam Basin in China.";
RL Stand. Genomic Sci. 10:116-116(2015).
RN [2] {ECO:0000313|Proteomes:UP000034029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3B36 {ECO:0000313|Proteomes:UP000034029};
RA Ma Y., Jiang K., Xue Y.;
RT "Complete genome sequence of Salinicoccus halodurans strain H3B36, isolated
RT from the Qaidam basin of China.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFK65465.1, ECO:0000313|Proteomes:UP000183090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6501 {ECO:0000313|EMBL:SFK65465.1,
RC ECO:0000313|Proteomes:UP000183090};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; CP011366; AKG75078.1; -; Genomic_DNA.
DR EMBL; FOTB01000002; SFK65465.1; -; Genomic_DNA.
DR RefSeq; WP_046791255.1; NZ_FOTB01000002.1.
DR AlphaFoldDB; A0A0F7HNC0; -.
DR STRING; 407035.AAT16_13310; -.
DR KEGG; shv:AAT16_13310; -.
DR PATRIC; fig|407035.3.peg.2740; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000034029; Chromosome.
DR Proteomes; UP000183090; Unassembled WGS sequence.
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}; Hydrolase {ECO:0000313|EMBL:AKG75078.1};
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 10..204
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 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 395 AA; 43198 MW; 4619774392BB42FC CRC64;
MAKEKFDRSK THANIGTIGH VDHGKTTLTA AIATVLAKRG SGEAQSYAQI DNAPEEKERG
ITINTSHIEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GGILVVSAAD GPMPQTREHI
LLSRNVGVPA LVVFLNKVDM VDDEELLELV EMEVRELLSE YDFPGDDIPV IAGSALKALE
GVEEYENKIL ELMEAVDTYI PTPERDSDKP FMMPVEDVFS ITGRGTVATG RVDRGQIKVG
DEVEIIGLTE ESGKTTVTGV EMFRKLLDYA EAGDNIGALL RGVAREDIQR GQVLAKPGSI
TPHTNFKAEV YVLSKEEGGR HTPFFNNYRP QFYFRTTDVT GVVNLPEGTE MVMPGDNVEM
TVELISPIAI EDGTRFSIRE GGRTVGSGVV TDIIK
//
