GenomeNet

Database: UniProt/TrEMBL
Entry: F7Z1B7_BACC6
LinkDB: F7Z1B7_BACC6
Original site: F7Z1B7_BACC6 
ID   F7Z1B7_BACC6            Unreviewed;       395 AA.
AC   F7Z1B7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   23-MAY-2018, entry version 44.
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   OrderedLocusNames=BCO26_0117 {ECO:0000313|EMBL:AEH52176.1};
OS   Bacillus coagulans (strain 2-6).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=941639 {ECO:0000313|EMBL:AEH52176.1, ECO:0000313|Proteomes:UP000005637};
RN   [1] {ECO:0000313|EMBL:AEH52176.1, ECO:0000313|Proteomes:UP000005637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-6 {ECO:0000313|EMBL:AEH52176.1,
RC   ECO:0000313|Proteomes:UP000005637};
RX   PubMed=21705584; DOI=10.1128/JB.05378-11;
RA   Su F., Yu B., Sun J., Ou H.Y., Zhao B., Wang L., Qin J., Tang H.,
RA   Tao F., Jarek M., Scharfe M., Ma C., Ma Y., Xu P.;
RT   "Genome sequence of the thermophilic strain Bacillus coagulans 2-6, an
RT   efficient producer of high-optical-purity L-lactic acid.";
RL   J. Bacteriol. 193:4563-4564(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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002472; AEH52176.1; -; Genomic_DNA.
DR   RefSeq; WP_013858077.1; NC_015634.1.
DR   EnsemblBacteria; AEH52176; AEH52176; BCO26_0117.
DR   KEGG; bck:BCO26_0117; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000005637; 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:UP000005637};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AEH52176.1};
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   395 AA;  43337 MW;  FCEF2718A8B47647 CRC64;
     MAKQKFDRSK EHCNIGTIGH VDHGKTTLTA AITAVLAKQG KAEARAYDQI DGAPEERERG
     ITINTAHVEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKCDM VDDEELLELV EMEVRDLLSE YDFPGDEVPV IKGSALKALE
     GDPEYEAKIL ELMDAVDEYI PTPQRDTDKP FMMPVEDVFS ITGRGTVATG RVERGQLKVG
     DVVEIVGLSD KPKQTTVTGV EMFRKILDYA EAGDNIGALL RGIAREEVQR GQVLAKPGSI
     TPHTKFKAQV YVLTKEEGGR HTPFFSNYRP QFYFRTTDVT GIITLPEGVE MVMPGDNVEM
     SVELIAPIAI EEGTKFSIRE GGRTVGAGSV SSIEA
//
DBGET integrated database retrieval system