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Database: UniProt/TrEMBL
Entry: A0A0U1HY29_YERRO
LinkDB: A0A0U1HY29_YERRO
Original site: A0A0U1HY29_YERRO 
ID   A0A0U1HY29_YERRO        Unreviewed;       394 AA.
AC   A0A0U1HY29;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-MAR-2018, entry version 17.
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=tufA_2 {ECO:0000313|EMBL:CQI97549.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=ERS008555_03916 {ECO:0000313|EMBL:CQI97549.1};
OS   Yersinia rohdei.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=29485 {ECO:0000313|EMBL:CQI97549.1, ECO:0000313|Proteomes:UP000042054};
RN   [1] {ECO:0000313|EMBL:CQI97549.1, ECO:0000313|Proteomes:UP000042054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68/02 {ECO:0000313|EMBL:CQI97549.1,
RC   ECO:0000313|Proteomes:UP000042054};
RA   Murphy D.;
RL   Submitted (MAR-2015) 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; CTKE01000030; CQI97549.1; -; Genomic_DNA.
DR   RefSeq; WP_004716473.1; NZ_CTKU01000036.1.
DR   ProteinModelPortal; A0A0U1HY29; -.
DR   EnsemblBacteria; CQI97549; CQI97549; ERS008555_03916.
DR   KEGG; yro:CH64_2877; -.
DR   KO; K02358; -.
DR   Proteomes; UP000042054; 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:UP000042054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CQI97549.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:CQI97549.1};
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;  43212 MW;  9A92CDCB51F9A4D8 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGSARAFDQI DNAPEEKARG
     ITINTSHVEY DTPARHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY ILVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPV IRGSALKALE
     GEAEWEAKII ELAEALDSYI PQPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIVRVG
     EEVEIVGIID TIKTTCTGVE MFRKLLDEGR AGENVGVLLR GTKRDDVQRG QVLAKPGSIK
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPDGVEM VMPGDNIQMI
     VNLIAPIAMD DGLRFAIREG GRTVGAGVVA KVIE
//
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