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Database: UniProt/TrEMBL
Entry: R4Y5C1_KLEPR
LinkDB: R4Y5C1_KLEPR
Original site: R4Y5C1_KLEPR 
ID   R4Y5C1_KLEPR            Unreviewed;       394 AA.
AC   R4Y5C1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   22-NOV-2017, entry version 40.
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=ef-tu {ECO:0000313|EMBL:CCI74978.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=KPR_0748 {ECO:0000313|EMBL:CCI74978.1};
OS   Klebsiella pneumoniae subsp. rhinoscleromatis SB3432.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=861365 {ECO:0000313|Proteomes:UP000013942};
RN   [1] {ECO:0000313|EMBL:CCI74978.1, ECO:0000313|Proteomes:UP000013942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3432 {ECO:0000313|EMBL:CCI74978.1,
RC   ECO:0000313|Proteomes:UP000013942};
RX   PubMed=21629720; DOI=10.1371/journal.pntd.0001052;
RG   Institut Pasteur;
RG   Genotyping of Pathogens and Public Health;
RG   and Genomic analysis and integration;
RG   and Unite de Pathogenie Microbienne Moleculaire;
RG   and Unite INSERM U786;
RG   28 rue du Dr ROUX;
RG   75724 Paris;
RG   France. CEA-IG;
RG   Genoscope;
RG   91057 Evry;
RG   France.;
RA   Fevre C., Passet V., Deletoile A., Barbe V., Frangeul L.,
RA   Almeida A.S., Sansonetti P., Tournebize R., Brisse S.;
RT   "PCR-based identification of Klebsiella pneumoniae subsp.
RT   rhinoscleromatis, the agent of rhinoscleroma.";
RL   PLoS Negl. Trop. Dis. 5:e1052-e1052(2011).
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; FO203501; CCI74978.1; -; Genomic_DNA.
DR   RefSeq; WP_004174069.1; NC_021232.1.
DR   ProteinModelPortal; R4Y5C1; -.
DR   SMR; R4Y5C1; -.
DR   EnsemblBacteria; CCI74978; CCI74978; KPR_0748.
DR   KEGG; kpr:KPR_0748; -.
DR   PATRIC; fig|861365.4.peg.1985; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   Proteomes; UP000013942; 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:UP000013942};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118};
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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