ID A0A1A9F485_9GAMM Unreviewed; 407 AA.
AC A0A1A9F485;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=A8C75_21450 {ECO:0000313|EMBL:ANG64790.1}, A8C75_21515
GN {ECO:0000313|EMBL:ANG64802.1};
OS Marinobacterium aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG64790.1, ECO:0000313|Proteomes:UP000078070};
RN [1] {ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA Baek K., Yang S.-J.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANG64790.1, ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|EMBL:ANG64790.1,
RC ECO:0000313|Proteomes:UP000078070};
RX PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA Bae S.S., Jung J., Chung D., Baek K.;
RT "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT isolated from estuary sediment.";
RL Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
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; CP015839; ANG64790.1; -; Genomic_DNA.
DR EMBL; CP015839; ANG64802.1; -; Genomic_DNA.
DR RefSeq; WP_067386410.1; NZ_CP015839.1.
DR AlphaFoldDB; A0A1A9F485; -.
DR STRING; 1821621.A8C75_21450; -.
DR KEGG; mars:A8C75_21450; -.
DR KEGG; mars:A8C75_21515; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000078070; 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:UP000078070}.
FT DOMAIN 10..217
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 407 AA; 44147 MW; D4636669EAA31E6D CRC64;
MGKKAFERNK PHVNVGTIGH VDHGKTTLTA ALTRVCSETW GGSAVAFDGI DNAPEERERG
ITIATSHVEY ESPSRHYAHV DCPGHADYVK NMITGAAQMD GAILVCGATD GPMPQTREHI
LLSRQVGVPF IVVFLNKADL LAEDCGGVES EEYAEMLELV EMELRELLDA YDFPGDDTPI
IAGSALMALN GQDDNELGTS AVLKLVDALD NYIPQPERAI DLPFLMPVED VFSISGRGTV
VTGRVERGIL KVGDQIEIVG VRDTQVTTCT GVEMFRKLLD EGRAGENVGA LLRGTKRDDV
ERGQVLCKPG SIKPHTQFEG EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD ITGACELPEG
VEMVMPGDNV QMSVTLINPI AMEEGLRFAI REGGRTVGAG VVAKIIA
//