ID A0A060UQM1_9PROT Unreviewed; 396 AA.
AC A0A060UQM1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:CDQ10745.1};
GN ORFNames=AFERRI_420043 {ECO:0000313|EMBL:CDQ10745.1}, BBC27_04695
GN {ECO:0000313|EMBL:OCB01310.1}, H2515_02495
GN {ECO:0000313|EMBL:QQD73210.1}, H2515_02560
GN {ECO:0000313|EMBL:QQD73222.1};
OS Acidithiobacillus ferrivorans.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=160808 {ECO:0000313|EMBL:CDQ10745.1, ECO:0000313|Proteomes:UP000029069};
RN [1] {ECO:0000313|EMBL:CDQ10745.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ10745.1};
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ10745.1, ECO:0000313|Proteomes:UP000029069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ10745.1,
RC ECO:0000313|Proteomes:UP000029069};
RA Talla E., Hedrich S., Mangenot S., Ji B., Johnson D.B., Barbe V.,
RA Bonnefoy V.;
RT "Initial genome analysis of the psychrotolerant acidophile
RT Acidithiobacillus ferrivorans CF27: insights into iron and sulfur oxidation
RT pathways and into biofilm formation.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OCB01310.1, ECO:0000313|Proteomes:UP000093129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL15 {ECO:0000313|EMBL:OCB01310.1,
RC ECO:0000313|Proteomes:UP000093129};
RA Peng T., Ma L., Nan M., An N., Wang M., Qiu G., Zeng W.;
RT "Draft genome of a psychrotolerant acidophile Acidithiobacillus ferrivorans
RT strain YL15.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QQD73210.1, ECO:0000313|Proteomes:UP000595420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XJFY6S-08 {ECO:0000313|EMBL:QQD73210.1,
RC ECO:0000313|Proteomes:UP000595420};
RA Yan L., Ni Y.;
RT "Complete genome sequence analysis of Acidithiobacillus ferrivorans XJFY6S-
RT 08 reveals extreme environmental adaptation to alpine acid mine drainage.";
RL Submitted (JUL-2020) 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; CCCS020000037; CDQ10745.1; -; Genomic_DNA.
DR EMBL; MASQ01000162; OCB01310.1; -; Genomic_DNA.
DR EMBL; CP059488; QQD73210.1; -; Genomic_DNA.
DR EMBL; CP059488; QQD73222.1; -; Genomic_DNA.
DR RefSeq; WP_014030034.1; NZ_MASQ01000162.1.
DR OrthoDB; 5288748at2; -.
DR Proteomes; UP000029069; Unassembled WGS sequence.
DR Proteomes; UP000093129; Unassembled WGS sequence.
DR Proteomes; UP000595420; 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}.
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; 43238 MW; D06094C099EA1D04 CRC64;
MSKGKFERTK PHVNVGTIGH VDHGKTTLTA ALTKVLSAKF GGEVRAYDQI DNAPEERARG
ITIATSHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
LLARQVGVPF IVVFLNKADM VDDAELLELV EMEVRELLVK YEFPGDDIPV IIGSALKALE
GDQSDIGEPA IFRLAEAMDS YIPMPERPID KPFLMPIEDV FSISGRGTVV TGRIERGIVK
IGDEIEIIGI RDTVKSIVTG VEMFRKILDQ GQAGDNVGVL LRGTKKDDVE RGQVLAKPGS
IKPHTRFEAE VYVLSKEEGG RHTPFFNGYR PQFYFRTTDV TGAVELPEGV EMVMPGDNIL
FKVALIAPIA MEEGLRFAVR EGGRTVGAGV VSKVVE
//
