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Database: UniProt
Entry: D9QGT6_BRESC
LinkDB: D9QGT6_BRESC
Original site: D9QGT6_BRESC 
ID   D9QGT6_BRESC            Unreviewed;       396 AA.
AC   D9QGT6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=Bresu_1591 {ECO:0000313|EMBL:ADL00902.1}, Bresu_1794
GN   {ECO:0000313|EMBL:ADL01105.1};
OS   Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS   NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL00902.1, ECO:0000313|Proteomes:UP000002696};
RN   [1] {ECO:0000313|EMBL:ADL00902.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 15264 {ECO:0000313|EMBL:ADL00902.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Zhang X., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Brown P.J.B., Brun Y.V., Woyke T.;
RT   "Complete sequence of Brevundimonas subvibrioides ATCC 15264.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC   {ECO:0000313|Proteomes:UP000002696};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(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; CP002102; ADL00902.1; -; Genomic_DNA.
DR   EMBL; CP002102; ADL01105.1; -; Genomic_DNA.
DR   RefSeq; WP_013269004.1; NC_014375.1.
DR   AlphaFoldDB; D9QGT6; -.
DR   STRING; 633149.Bresu_1591; -.
DR   KEGG; bsb:Bresu_1591; -.
DR   KEGG; bsb:Bresu_1794; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_5; -.
DR   InParanoid; D9QGT6; -.
DR   OrthoDB; 9803139at2; -.
DR   BioCyc; BSUB633149:G1GM8-1581-MONOMER; -.
DR   BioCyc; BSUB633149:G1GM8-1787-MONOMER; -.
DR   Proteomes; UP000002696; 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:UP000002696}.
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;  43099 MW;  2E2A3E7AD61C192E CRC64;
     MAKEKFERNK PHCNIGTIGH VDHGKTTLTA AITMTLAKAG GAKAMAYADI DAAPEEKARG
     ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFMNKVDL VDDKELLELV EMEVRELLSS YQFPGDDIPI TMGSAKAATD
     GVNPEIGEQQ VLALMETVDA YIPQPERPVD LPFLMPVEDV FSISGRGTVV TGRVERGIVK
     VGEEVEIVGI RPVQKTTCTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVE RGQVLCKPGS
     ITPHTKFLAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGIVHLKEGV EMIMPGDNAE
     LNVELITPIA MEEKLRFAIR EGGRTVGAGV VAKIIA
//
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