ID A0A0H3CDX8_ENTCC Unreviewed; 394 AA.
AC A0A0H3CDX8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=ECL_00237 {ECO:0000313|EMBL:ADF59804.1};
OS Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC
OS 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=716541 {ECO:0000313|EMBL:ADF59804.1, ECO:0000313|Proteomes:UP000002363};
RN [1] {ECO:0000313|EMBL:ADF59804.1, ECO:0000313|Proteomes:UP000002363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 /
RC NCDC 279-56 {ECO:0000313|Proteomes:UP000002363};
RX PubMed=20207761; DOI=10.1128/JB.00067-10;
RA Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT strain ATCC 13047.";
RL J. Bacteriol. 192:2463-2464(2010).
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; CP001918; ADF59804.1; -; Genomic_DNA.
DR RefSeq; WP_013094997.1; NC_014121.1.
DR RefSeq; YP_003610753.1; NC_014121.1.
DR AlphaFoldDB; A0A0H3CDX8; -.
DR STRING; 716541.ECL_00237; -.
DR EnsemblBacteria; ADF59804; ADF59804; ECL_00237.
DR GeneID; 83571542; -.
DR KEGG; enc:ECL_00237; -.
DR PATRIC; fig|716541.4.peg.525; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_2_6; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000002363; 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}.
FT DOMAIN 10..204
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 394 AA; 43244 MW; 87179C0092355C91 CRC64;
MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGSARAFDQI DNAPEEKARG
ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
GDAEWEAKII ELAGYLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
EEVEIVGIKE TAKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGSIK
PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
//