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Database: UniProt/TrEMBL
Entry: A0A0G3RZR7_KLEOX
LinkDB: A0A0G3RZR7_KLEOX
Original site: A0A0G3RZR7_KLEOX 
ID   A0A0G3RZR7_KLEOX        Unreviewed;       394 AA.
AC   A0A0G3RZR7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   22-NOV-2017, entry version 20.
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   ECO:0000313|EMBL:AKL33454.1};
GN   Synonyms=tuf1 {ECO:0000313|EMBL:SBL22374.1};
GN   ORFNames=AB185_05825 {ECO:0000313|EMBL:AKL33454.1}, AB185_09355
GN   {ECO:0000313|EMBL:AKL34094.1}, SAMEA2273697_00046
GN   {ECO:0000313|EMBL:SBL22374.1};
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=571 {ECO:0000313|EMBL:AKL33454.1, ECO:0000313|Proteomes:UP000035545};
RN   [1] {ECO:0000313|EMBL:AKL33454.1, ECO:0000313|Proteomes:UP000035545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAV1374 {ECO:0000313|EMBL:AKL33454.1,
RC   ECO:0000313|Proteomes:UP000035545};
RA   Sheppard A.E., Stoesser N., Wilson D., Sebra R., Kasarskis A.,
RA   Anson L., Giess A., Pankhurst L., Vaughan A., Grim C.J., Cox H.,
RA   Yeh A., Sifri C.D., Walker S., Peto T.E., Crook D.W., Mathers A.J.;
RT   "Rapid spread of a carbapenem resistance gene driven by multiple
RT   levels of genetic mobility.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SBL22374.1, ECO:0000313|Proteomes:UP000077898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2880STDY5682622 {ECO:0000313|EMBL:SBL22374.1,
RC   ECO:0000313|Proteomes:UP000077898};
RG   Pathogen Informatics;
RL   Submitted (MAY-2016) 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; CP011636; AKL33454.1; -; Genomic_DNA.
DR   EMBL; CP011636; AKL34094.1; -; Genomic_DNA.
DR   EMBL; FLAB01000001; SBL22374.1; -; Genomic_DNA.
DR   RefSeq; WP_004097636.1; NZ_JWBI01000226.1.
DR   EnsemblBacteria; AKL33454; AKL33454; AB185_05825.
DR   EnsemblBacteria; AKL34094; AKL34094; AB185_09355.
DR   EnsemblBacteria; SBL22374; SBL22374; SAMEA2273697_00046.
DR   GeneID; 29379931; -.
DR   KEGG; koc:AB185_05825; -.
DR   KEGG; koc:AB185_09355; -.
DR   PATRIC; fig|571.110.peg.208; -.
DR   KO; K02358; -.
DR   Proteomes; UP000035545; Chromosome.
DR   Proteomes; UP000077898; Unassembled WGS sequence.
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:UP000035545,
KW   ECO:0000313|Proteomes:UP000077898};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AKL33454.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:AKL33454.1};
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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