ID A0A0Q9YRI7_9COXI Unreviewed; 394 AA.
AC A0A0Q9YRI7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=tufA {ECO:0000313|EMBL:KRG19057.1};
GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN ORFNames=CC99x_01048 {ECO:0000313|EMBL:KRG19057.1};
OS Candidatus Berkiella cookevillensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG19057.1, ECO:0000313|Proteomes:UP000051494};
RN [1] {ECO:0000313|EMBL:KRG19057.1, ECO:0000313|Proteomes:UP000051494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC99 {ECO:0000313|EMBL:KRG19057.1,
RC ECO:0000313|Proteomes:UP000051494};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG19057.1}.
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DR EMBL; LKHV01000004; KRG19057.1; -; Genomic_DNA.
DR RefSeq; WP_057624169.1; NZ_LKHV02000001.1.
DR AlphaFoldDB; A0A0Q9YRI7; -.
DR STRING; 437022.CC99x_01048; -.
DR PATRIC; fig|1590042.3.peg.1067; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000051494; 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: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:UP000051494}.
FT DOMAIN 8..204
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 79..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 394 AA; 42856 MW; 8BA82FEB03593B23 CRC64;
MAEFQRTKPH VNVGTIGHVD HGKTTLTAAI TKVLASKGQA QFVDYANIDK APEERERGIT
ISTSHVEYES DNRHYAHVDC PGHADYVKNM ITGAAQMDGA ILVCSAADGP MPQTREHILL
ARQVGVPHIV VFLNKADMVD DAELLELVEM EVRDLLSSYG FPGDDIPIIT GSALKALEGD
TSDIGEGAIY KLVEAMDSYF PLPTREVDKP FLLPVEDVFS ISGRGTVVTG RIERGIVKVG
EEIEIIGLKD TVKTTVTGVE MFRKMLKEGQ AGDNVGLLLR GTKREDVERG QVLAAPKSIT
PHTKFQAEIY VLSKEEGGRR TPFLSGYRPQ FYFRTTDVTG MIDLPEGTEM VMPGDNITVT
VTLISPIAME DGLKFAIREG GKTVGAGVVA KIID
//
