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Database: UniProt/TrEMBL
Entry: A0A0E1C7K3_KLEPN
LinkDB: A0A0E1C7K3_KLEPN
Original site: A0A0E1C7K3_KLEPN 
ID   A0A0E1C7K3_KLEPN        Unreviewed;       394 AA.
AC   A0A0E1C7K3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-MAR-2018, entry version 19.
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=KPNJ1_00414 {ECO:0000313|EMBL:AHM82820.1}, KPNJ1_05241
GN   {ECO:0000313|EMBL:AHM87637.1};
OS   Klebsiella pneumoniae 30660/NJST258_1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1420012 {ECO:0000313|EMBL:AHM82820.1, ECO:0000313|Proteomes:UP000019583};
RN   [1] {ECO:0000313|EMBL:AHM82820.1, ECO:0000313|Proteomes:UP000019583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30660/NJST258_1 {ECO:0000313|EMBL:AHM82820.1,
RC   ECO:0000313|Proteomes:UP000019583};
RX   PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA   Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA   Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J.,
RA   Bonomo R.A., Musser J.M., Kreiswirth B.N.;
RT   "Molecular dissection of the evolution of carbapenem-resistant
RT   multilocus sequence type 258 Klebsiella pneumoniae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
RN   [2] {ECO:0000313|EMBL:AHM82820.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=30660/NJST258_1 {ECO:0000313|EMBL:AHM82820.1};
RA   DeLeo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA   Porter A.R., Chavda K.D., Jacob M., Mathema B., Olsen R.J.,
RA   Musser J.M., Bonomo R., Kreiswirth B.N.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; CP006923; AHM82820.1; -; Genomic_DNA.
DR   EMBL; CP006923; AHM87637.1; -; Genomic_DNA.
DR   RefSeq; WP_004174069.1; NZ_CP006923.1.
DR   ProteinModelPortal; A0A0E1C7K3; -.
DR   SMR; A0A0E1C7K3; -.
DR   EnsemblBacteria; AHM82820; AHM82820; KPNJ1_00414.
DR   EnsemblBacteria; AHM87637; AHM87637; KPNJ1_05241.
DR   KEGG; kpa:KPNJ1_00414; -.
DR   KEGG; kpa:KPNJ1_05241; -.
DR   PATRIC; fig|1420012.3.peg.394; -.
DR   KO; K02358; -.
DR   Proteomes; UP000019583; 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:UP000019583};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AHM82820.1};
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;  43246 MW;  DBA4133541205DD8 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 QVLAKPGTIN
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
     VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG
//
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