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Database: UniProt/TrEMBL
Entry: W0U4I0_9FIRM
LinkDB: W0U4I0_9FIRM
Original site: W0U4I0_9FIRM 
ID   W0U4I0_9FIRM            Unreviewed;       399 AA.
AC   W0U4I0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   28-MAR-2018, entry version 24.
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:CCO04457.1};
GN   ORFNames=RBI_I00734 {ECO:0000313|EMBL:CCO04457.1};
OS   Ruminococcus bicirculans.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1160721 {ECO:0000313|EMBL:CCO04457.1, ECO:0000313|Proteomes:UP000027600};
RN   [1] {ECO:0000313|EMBL:CCO04457.1, ECO:0000313|Proteomes:UP000027600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=80/3 {ECO:0000313|EMBL:CCO04457.1};
RX   PubMed=23919528; DOI=10.1111/1462-2920.12217;
RA   Wegmann U., Louis P., Goesmann A., Henrissat B., Duncan S.H.,
RA   Flint H.J.;
RT   "Complete genome of a new Firmicutes species belonging to the dominant
RT   human colonic microbiota ('Ruminococcus bicirculans') reveals two
RT   chromosomes and a selective capacity to utilize plant glucans.";
RL   Environ. Microbiol. 16:2879-2890(2014).
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; HF545616; CCO04457.1; -; Genomic_DNA.
DR   RefSeq; WP_022288661.1; NZ_HF545616.1.
DR   EnsemblBacteria; CCO04457; CCO04457; RBI_I00734.
DR   KEGG; rus:RBI_I00734; -.
DR   KO; K02358; -.
DR   Proteomes; UP000027600; Chromosome I.
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:UP000027600};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CCO04457.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:CCO04457.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   DOMAIN       10    208       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   399 AA;  43874 MW;  F579FD91CB9E389B CRC64;
     MAKAHFERTK PHVNIGTIGH VDHGKTTLTA AITKTLALEG LAEKKDYNNI DSAPEERERG
     ITINTAHVEY ETKNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAASD GPMAQTREHL
     LLARQVGVPA IVVFMNKADQ VDDEELLDLV EMDIRELLDK YDFPGDETPI IKGSALAALE
     APDDLSDPAY KPILDLMDAV DTFIPTPDRK SDLPFLMPVE DVFTITGRGT VATGRVERGQ
     LKTGDEVEIL GLSTERPKTV VTGIEMFRKI LDYAEAGDNI GALLRGIQRS DIQRGQVLCK
     PGSIHPYTKF SGQVYVLKKE EGGRHTPFFN NYRPQFYFRT TDVTGVITLP ADKEMCMPGD
     NVEMDVELIT PIAIEEGLRF AIREGGRTVG SGVVTAVRD
//
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