ID A0A0M4NXK5_9GAMM Unreviewed; 396 AA.
AC A0A0M4NXK5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:ALE52789.1};
GN ORFNames=SP60_05230 {ECO:0000313|EMBL:ALE52656.1}, SP60_05990
GN {ECO:0000313|EMBL:ALE52789.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52789.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE52789.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52789.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
RN [2] {ECO:0000313|EMBL:ALE52789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52789.1};
RX PubMed=27434424;
RA Shah V., Chang B.X., Morris R.M.;
RT "Cultivation of a chemoautotroph from the SUP05 clade of marine bacteria
RT that produces nitrite and consumes ammonium.";
RL ISME J. 0:0-0(2016).
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; CP010552; ALE52656.1; -; Genomic_DNA.
DR EMBL; CP010552; ALE52789.1; -; Genomic_DNA.
DR RefSeq; WP_053951621.1; NZ_CP010552.1.
DR AlphaFoldDB; A0A0M4NXK5; -.
DR STRING; 1705394.SP60_05230; -.
DR KEGG; tho:SP60_05230; -.
DR KEGG; tho:SP60_05990; -.
DR PATRIC; fig|1705394.5.peg.1045; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000058020; 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}; Hydrolase {ECO:0000313|EMBL:ALE52789.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000058020}.
FT DOMAIN 10..206
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 396 AA; 43220 MW; DCA0EA7806D5307C CRC64;
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITKVMAEAN GSEATDFADI DKAPEERERG
ITISTSHVEY ESETRHYAHV DCPGHADYVK NMITGAAQMD GAIIVIAATD GPMAQTREHI
LLSKQVGVPY IVVYMNKADM VDDEELIELV EMEIRELLNE YDFPGDDTPV ILGSALKALE
GDTSDIGVPS VLKLVEALDT YIPEPVRDTE KTFIMPIEDV FSISGRGTVV TGRIEAGIVN
VGDELEIVGI KDTQTTTCTG VEMFRKLLDS GEAGDNVGVL LRGTKREEVE RGQVLAKPGS
IKPHSKFEAE VYVLSKDEGG RHTPFFDNYR PQFYFRTTDV TGACKLPDGV EMVMPGDNVK
MQVELLSPIA MEDGLRFAIR EGGRTVGAGV VSKVTD
//
