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Database: UniProt/TrEMBL
Entry: A0A0C7KSV1_KLEVA
LinkDB: A0A0C7KSV1_KLEVA
Original site: A0A0C7KSV1_KLEVA 
ID   A0A0C7KSV1_KLEVA        Unreviewed;       394 AA.
AC   A0A0C7KSV1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   05-JUL-2017, entry version 16.
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   ORFNames=BBD63_01065 {ECO:0000313|EMBL:AQL13908.1}, BBD64_01065
GN   {ECO:0000313|EMBL:AQL18994.1}, BBD65_01065
GN   {ECO:0000313|EMBL:AQL24760.1};
OS   Klebsiella variicola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=244366 {ECO:0000313|EMBL:AQL13908.1, ECO:0000313|Proteomes:UP000188029};
RN   [1] {ECO:0000313|EMBL:AQL18994.1, ECO:0000313|Proteomes:UP000187763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GJ2 {ECO:0000313|EMBL:AQL18994.1,
RC   ECO:0000313|Proteomes:UP000187763};
RA   Di D.Y.W., Jang J., Unno T., Hur H.-G.;
RT   "Emergence of NDM-9, a variant of New Delhi Metallo-Beta-lactam-
RT   Positive Klebsiella variicola in an Urban River in South Korea.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AQL13908.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GJ1 {ECO:0000313|EMBL:AQL13908.1}, and GJ3
RC   {ECO:0000313|EMBL:AQL24760.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AQL13908.1, ECO:0000313|Proteomes:UP000187818, ECO:0000313|Proteomes:UP000188029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GJ1 {ECO:0000313|EMBL:AQL13908.1,
RC   ECO:0000313|Proteomes:UP000188029}, and GJ3
RC   {ECO:0000313|EMBL:AQL24760.1, ECO:0000313|Proteomes:UP000187818};
RX   PubMed=28087584;
RA   Di D.Y., Jang J., Unno T., Hur H.G.;
RT   "Emergence of Klebsiella variicola positive for NDM-9, a variant of
RT   New Delhi metallo-beta-lactamase, in an urban river in South Korea.";
RL   J. Antimicrob. Chemother. 0:0-0(2017).
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; CP017284; AQL13908.1; -; Genomic_DNA.
DR   EMBL; CP017849; AQL18994.1; -; Genomic_DNA.
DR   EMBL; CP017289; AQL24760.1; -; Genomic_DNA.
DR   RefSeq; WP_012543214.1; NZ_MPCI01000001.1.
DR   KEGG; kvd:KR75_09320; -.
DR   KEGG; kvq:SP68_15910; -.
DR   KO; K02358; -.
DR   Proteomes; UP000187763; Chromosome.
DR   Proteomes; UP000187818; Chromosome.
DR   Proteomes; UP000188029; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
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.
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:UP000187763,
KW   ECO:0000313|Proteomes:UP000187818, ECO:0000313|Proteomes:UP000188029};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AQL13908.1};
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 (guanine nucleotide-binding).
FT                                {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;  43246 MW;  D8F6771304440D9D CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGSARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
     GDAEWEAKII ELAGHLDTYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
     EEVEIVGIKE TAKTTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGSIK
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
     VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
//
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