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Database: UniProt
Entry: A0A0H3XGS2_9MOLU
LinkDB: A0A0H3XGS2_9MOLU
Original site: A0A0H3XGS2_9MOLU 
ID   A0A0H3XGS2_9MOLU        Unreviewed;       394 AA.
AC   A0A0H3XGS2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   28-MAR-2018, entry version 22.
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 {ECO:0000313|EMBL:AKM53688.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=SERIO_v1c00860 {ECO:0000313|EMBL:AKM53688.1};
OS   Spiroplasma eriocheiris.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales;
OC   Spiroplasmataceae; Spiroplasma.
OX   NCBI_TaxID=315358 {ECO:0000313|EMBL:AKM53688.1, ECO:0000313|Proteomes:UP000035661};
RN   [1] {ECO:0000313|Proteomes:UP000035661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RA   Lo W.-S., Kuo C.-H.;
RT   "Complete genome sequence of Spiroplasma eriocheiris TDA-040725-5 (DSM
RT   21848).";
RL   Submitted (JUN-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; CP011856; AKM53688.1; -; Genomic_DNA.
DR   RefSeq; WP_047790972.1; NZ_CP011856.1.
DR   EnsemblBacteria; AKM53688; AKM53688; SERIO_v1c00860.
DR   KEGG; seri:SERIO_v1c00860; -.
DR   PATRIC; fig|743698.3.peg.88; -.
DR   KO; K02358; -.
DR   Proteomes; UP000035661; 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:UP000035661};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AKM53688.1};
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:UP000035661}.
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;  43235 MW;  B5E860CC2760A19C CRC64;
     MAKQKFDRSL PHVNVGTIGH VDHGKTTLTA AITTVLAKKG FAEAKGYDGI DNAPEEKERG
     ITINTSHVEY RTEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLSKQVGVPK IVVFLNKCDM VDDADLLDLV DMEVRDLLSQ YDFDGDNAPV IKGSALGALN
     GEPQWEEKVM ELMDAVDNYI PTPERDKDKP FLMPVEDVFT ITGRGTVATG RVERGELKLN
     DEVEIVGIKP THKTVVTGIE MFRKLLDYAE AGDNIGALLR GVDRDDIQRG QVLAKPGTVK
     PHQEFKAQVY ALTKEEGGRH TPFFGHYRPQ FYFRTTDVTG SIELPAGTEM VMPGDNVELT
     VKLISPIAVE QGTKFSIREG GRTIGAGSVV EIIK
//
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