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Database: UniProt/TrEMBL
Entry: F9ZM41_ACICS
LinkDB: F9ZM41_ACICS
Original site: F9ZM41_ACICS 
ID   F9ZM41_ACICS            Unreviewed;       396 AA.
AC   F9ZM41;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
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   OrderedLocusNames=Atc_0590 {ECO:0000313|EMBL:AEK57240.1}, Atc_0603
GN   {ECO:0000313|EMBL:AEK57252.1};
OS   Acidithiobacillus caldus (strain SM-1).
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK57252.1, ECO:0000313|Proteomes:UP000006135};
RN   [1] {ECO:0000313|EMBL:AEK57252.1, ECO:0000313|Proteomes:UP000006135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM-1 {ECO:0000313|EMBL:AEK57252.1,
RC   ECO:0000313|Proteomes:UP000006135};
RX   PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA   You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA   Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT   "Unraveling the Acidithiobacillus caldus complete genome and its central
RT   metabolisms for carbon assimilation.";
RL   J. Genet. Genomics 38:243-252(2011).
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; CP002573; AEK57240.1; -; Genomic_DNA.
DR   EMBL; CP002573; AEK57252.1; -; Genomic_DNA.
DR   RefSeq; WP_004867925.1; NC_015850.1.
DR   AlphaFoldDB; F9ZM41; -.
DR   STRING; 990288.Atc_0590; -.
DR   GeneID; 69614345; -.
DR   KEGG; acu:Atc_0590; -.
DR   KEGG; acu:Atc_0603; -.
DR   HOGENOM; CLU_007265_0_0_6; -.
DR   OMA; EGDKEWG; -.
DR   OrthoDB; 5288748at2; -.
DR   Proteomes; UP000006135; 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:UP000006135}.
FT   DOMAIN          10..209
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;  43178 MW;  BEA63E4E10510447 CRC64;
     MSKGKFERTK PHVNVGTIGH VDHGKTTLTA ALTKVLSAKF GGEARAYDQI DNAPEERARG
     ITIATSHVEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPY IVVFMNKADM VDDAELLELV EMEVRELLSK YDFPGDDIPV VIGSALKALE
     GDQSDIGEPA IFKLAAAMDS YIPMPERPID KTFLMPIEDV FSISGRGTVV TGRIERGIVK
     VGDEIEIVGL RPTSKTTVTG VEMFRKILDQ GQAGDNVGVL LRGTKKDEVE RGQVLAKPGS
     IKPHTRFEAE VYVLSKEEGG RHTPFFNGYR PQFYFRTTDV TGAVELPEGV EMVMPGDNIQ
     FKVTLIAPIA MEEGLRFAVR EGGRTVGAGV VSKVVE
//
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