ID A0A099G0Q0_9RHOB Unreviewed; 391 AA.
AC A0A099G0Q0; A0A099GAV2; A0A099GK94;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:KGJ23166.1};
GN ORFNames=HGN31_09290 {ECO:0000313|EMBL:QJD17036.1}, HGN31_09420
GN {ECO:0000313|EMBL:QJD17058.1}, IX56_03745
GN {ECO:0000313|EMBL:KGJ23166.1}, IX56_03865
GN {ECO:0000313|EMBL:KGJ23188.1}, SAMN05444276_1011128
GN {ECO:0000313|EMBL:SDW49209.1};
OS Paracoccus sanguinis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ23166.1, ECO:0000313|Proteomes:UP000029858};
RN [1] {ECO:0000313|EMBL:KGJ23166.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ23166.1,
RC ECO:0000313|Proteomes:UP000029858};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ23166.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ23166.1,
RC ECO:0000313|Proteomes:UP000029858};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SDW49209.1, ECO:0000313|Proteomes:UP000182944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29303 {ECO:0000313|EMBL:SDW49209.1,
RC ECO:0000313|Proteomes:UP000182944};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QJD17036.1, ECO:0000313|Proteomes:UP000503485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM2164 {ECO:0000313|EMBL:QJD17036.1,
RC ECO:0000313|Proteomes:UP000503485};
RA Wu V.;
RT "Genome-Wide Identification of 5-Methylcytosine Sites in Bacterial Genomes
RT By High-Throughput Sequencing of MspJI Restriction Fragments.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QJD17036.1, ECO:0000313|Proteomes:UP000503485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM2164 {ECO:0000313|EMBL:QJD17036.1,
RC ECO:0000313|Proteomes:UP000503485};
RA Fomenkov A., Anton B.P., Roberts R.J.;
RL Submitted (APR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRKQ01000010; KGJ23166.1; -; Genomic_DNA.
DR EMBL; JRKQ01000010; KGJ23188.1; -; Genomic_DNA.
DR EMBL; CP051542; QJD17036.1; -; Genomic_DNA.
DR EMBL; CP051542; QJD17058.1; -; Genomic_DNA.
DR EMBL; FNNA01000001; SDW49209.1; -; Genomic_DNA.
DR RefSeq; WP_036703025.1; NZ_JRKT01000013.1.
DR STRING; 1545044.SAMN05444276_1011128; -.
DR KEGG; psan:HGN31_09290; -.
DR KEGG; psan:HGN31_09420; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000029858; Unassembled WGS sequence.
DR Proteomes; UP000182944; Unassembled WGS sequence.
DR Proteomes; UP000503485; 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:KGJ23166.1};
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:UP000029858}.
FT DOMAIN 10..201
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 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ SEQUENCE 391 AA; 42927 MW; 968C684BFDFED40F CRC64;
MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AITKYFGEFK AYDQIDGAPE ERARGITIST
AHVEYESDAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VNAADGPMPQ TREHILLGRQ
VGIPYMVVYL NKVDQVDDEE LLELVEMEVR ELLSSYDYPG DDIPIIKGSA LAALEGRDPE
IGENSIRALI KAVDEYIPTP ERAVDQPFLM PIEDVFSISG RGTVVTGRVE RGAVNVGDEL
EIVGIRPTKK TTCTGVEMFR KLLDRGEAGD NIGALLRGVD RDGVERGQVL CKPGSVKPHT
KFEAEAYILT KEEGGRHTPF FANYRPQFYF RTTDVTGTVK LPEGTEMVMP GDNLKFEVEL
IAPIAMEEKL RFAIREGGRT VGAGVVSKIL A
//
