ID A0A143HJY4_9GAMM Unreviewed; 397 AA.
AC A0A143HJY4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:AMX01582.1};
GN ORFNames=A3224_02370 {ECO:0000313|EMBL:AMX01570.1}, A3224_02435
GN {ECO:0000313|EMBL:AMX01582.1}, SAMN05660479_03041
GN {ECO:0000313|EMBL:SFD06113.1}, SAMN05660479_03383
GN {ECO:0000313|EMBL:SFD19214.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX01582.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|EMBL:AMX01582.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|EMBL:AMX01582.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFD06113.1, ECO:0000313|Proteomes:UP000181967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19189 {ECO:0000313|EMBL:SFD06113.1,
RC ECO:0000313|Proteomes:UP000181967};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; CP014864; AMX01570.1; -; Genomic_DNA.
DR EMBL; CP014864; AMX01582.1; -; Genomic_DNA.
DR EMBL; FOKT01000010; SFD06113.1; -; Genomic_DNA.
DR EMBL; FOKT01000029; SFD19214.1; -; Genomic_DNA.
DR RefSeq; WP_067150963.1; NZ_JAPHQG010000016.1.
DR AlphaFoldDB; A0A143HJY4; -.
DR STRING; 252514.A3224_02370; -.
DR GeneID; 76606905; -.
DR KEGG; mthd:A3224_02370; -.
DR KEGG; mthd:A3224_02435; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000076077; Chromosome.
DR Proteomes; UP000181967; 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:UP000076077}.
FT DOMAIN 10..207
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 397 AA; 43345 MW; 0E51EDE55FDEA7F1 CRC64;
MAKEKFERSK PHVNVGTIGH VDHGKTTLTA ALTRVCSEVW GGQAVAFDGI DNAPEERERG
ITIATSHVEY ESPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI
LLSRQVGVPY IVVFLNKADM VDDEELLELV EMEVRELLDQ YEFPGDDTPI IVGSALMALN
GEDDNGLGTS AVKKLVETLD EYIPEPERAV DQPFLMPIED VFSISGRGTV VTGRVERGVL
KTGDEIEIVG IRETTSTTCT GVEMFRKLLD EGRAGENIGA LLRGTKRDEV ERGQVLAKPG
SITPHTKFQA EVYVLSKDEG GRHTPFFKGY RPQFYFRTTD VTGAVELPEG TEMVMPGDNV
QMTVTLIAPI AMEEGLRFAI REGGRTVGAG VVSKIIE
//
