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Database: UniProt/TrEMBL
Entry: C5ARV5_METEA
LinkDB: C5ARV5_METEA
Original site: C5ARV5_METEA 
ID   C5ARV5_METEA            Unreviewed;       396 AA.
AC   C5ARV5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-SEP-2017, entry version 62.
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:ACS42443.1};
GN   OrderedLocusNames=MexAM1_META1p4832 {ECO:0000313|EMBL:ACS42443.1};
OS   Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 /
OS   NCIMB 9133 / AM1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS42443.1, ECO:0000313|Proteomes:UP000009081};
RN   [1] {ECO:0000313|EMBL:ACS42443.1, ECO:0000313|Proteomes:UP000009081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC   {ECO:0000313|Proteomes:UP000009081};
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A.,
RA   Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C.,
RA   Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S.,
RA   Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G.,
RA   Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z.,
RA   Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J.,
RA   Medigue C., Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to
RT   investigate microbial metabolism of C1 compounds from natural and
RT   industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
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; CP001510; ACS42443.1; -; Genomic_DNA.
DR   RefSeq; WP_003606924.1; NC_012808.1.
DR   STRING; 272630.MexAM1_META1p4832; -.
DR   EnsemblBacteria; ACS42443; ACS42443; MexAM1_META1p4832.
DR   KEGG; mea:Mex_1p4832; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   Proteomes; UP000009081; 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.
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:UP000009081};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ACS42443.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009081}.
FT   DOMAIN       10    206       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   396 AA;  43106 MW;  1E1425833A6E357B CRC64;
     MAKEKFSRTK PHCNIGTIGH VDHGKTSLTA AITKVLAESG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETTNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKVDM VDDEELLELV ELEVRELLSK YDFPGDDIPI TKGSALMALE
     DKEPKIGKEA VLALMATVDE YIPQPERPID MPFLMPIEDV FSISGRGTVV TGRVERGIVK
     VGESVEIVGI RPTTTTTVTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVE RGQVVCKPGS
     VKPHSKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVCTLPDGT EMVMPGDNVT
     MDVVLIVPVA MEEKLRFAIR EGGRTVGAGV VAAIND
//
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