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Database: UniProt/TrEMBL
Entry: A0A0H3H4Q2_KLEOK
LinkDB: A0A0H3H4Q2_KLEOK
Original site: A0A0H3H4Q2_KLEOK 
ID   A0A0H3H4Q2_KLEOK        Unreviewed;       394 AA.
AC   A0A0H3H4Q2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118, ECO:0000256|RuleBase:RU004061};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=KOX_04405 {ECO:0000313|EMBL:AEX02618.1}, KOX_07875
GN   {ECO:0000313|EMBL:AEX03303.1};
OS   Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC
OS   3318 / NRRL B-199 / KCTC 1686).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1006551 {ECO:0000313|EMBL:AEX03303.1, ECO:0000313|Proteomes:UP000007843};
RN   [1] {ECO:0000313|Proteomes:UP000007843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 /
RC   KCTC 1686 {ECO:0000313|Proteomes:UP000007843};
RA   Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT   "Complete genome sequence of Klebsiella oxytoca strain KCTC 1686.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEX03303.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KCTC 1686 {ECO:0000313|EMBL:AEX03303.1};
RX   PubMed=22493189; DOI=10.1128/JB.00026-12;
RA   Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA   Yang K.S.;
RT   "Complete Genome Sequence of Klebsiella oxytoca KCTC 1686, Used in
RT   Production of 2,3-Butanediol.";
RL   J. Bacteriol. 194:2371-2372(2012).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {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|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP003218; AEX02618.1; -; Genomic_DNA.
DR   EMBL; CP003218; AEX03303.1; -; Genomic_DNA.
DR   RefSeq; WP_004097636.1; NC_016612.1.
DR   STRING; 1006551.KOX_07875; -.
DR   EnsemblBacteria; AEX02618; AEX02618; KOX_04405.
DR   EnsemblBacteria; AEX03303; AEX03303; KOX_07875.
DR   GeneID; 29379931; -.
DR   KEGG; kox:KOX_04405; -.
DR   KEGG; kox:KOX_07875; -.
DR   PATRIC; fig|1006551.4.peg.1583; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   Proteomes; UP000007843; 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:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
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; TF_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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AEX03303.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   DOMAIN       10    204       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   394 AA;  43230 MW;  7CB78CDB288F2D4A CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGSARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
     GDADWEAKII ELAGYLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
     EEVEIVGIKE TAKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGSIK
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
     VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
//
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