ID A0A347UKR0_9RHOB Unreviewed; 391 AA.
AC A0A347UKR0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:AXX99438.1};
GN ORFNames=BAR1_00550 {ECO:0000313|EMBL:AXX96553.1}, BAR1_16770
GN {ECO:0000313|EMBL:AXX99438.1};
OS Profundibacter amoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Profundibacter.
OX NCBI_TaxID=2171755 {ECO:0000313|EMBL:AXX99438.1, ECO:0000313|Proteomes:UP000261704};
RN [1] {ECO:0000313|EMBL:AXX99438.1, ECO:0000313|Proteomes:UP000261704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAR1 {ECO:0000313|EMBL:AXX99438.1,
RC ECO:0000313|Proteomes:UP000261704};
RA Le Moine Bauer S., Sjoeberg A.G., L'Haridon S., Stokke R., Roalkvam I.,
RA Steen I.H., Dahle H.;
RT "Profundibacter amoris BAR1 gen. nov., sp. nov., a new member of the
RT Roseobacter clade isolated at Lokis Castle Vent Field on the Arctic Mid-
RT Oceanic Ridge.";
RL Submitted (SEP-2018) 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; CP032125; AXX96553.1; -; Genomic_DNA.
DR EMBL; CP032125; AXX99438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347UKR0; -.
DR KEGG; pamo:BAR1_00550; -.
DR KEGG; pamo:BAR1_16770; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000261704; 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:UP000261704}.
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; 42974 MW; 2B1EC58CA5AEBF18 CRC64;
MAKEKFERTK PHVNIGTIGH VDHGKTTLTA AITKYFGDFK GYDEIDGAPE EKARGITIST
AHVEYETETR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VNAADGPMPQ TREHILLGRQ
VGIPYMVVYM NKVDQVDDEE LLELVEMEIR ELLSSYDYPG DDIPVIPGSA LAALEGRDPE
IGEESIKKLM AAIDEYIPTP ERAVDQPFLM PIEDVFSISG RGTVVTGRIE RGVINVGDEI
EIVGIRDTSK TTCTGVEMFR KLLDRGEAGD NVGVLLRGID RDGVERGQIL CKPGSVTPHT
KFEAEAYILT KDEGGRHTPF FANYRPQFYF RTTDVTGTVT LPEGTEMVMP GDNLKFEVEL
IAPIAMEDGL RFAIREGGRT VGAGVVSKII E
//
