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EFTU_CHLT2
ID   EFTU_CHLT2              Reviewed;         394 AA.
AC   B0B7N8; O84324; P26622;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=CTL0574;
OS   Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1398121; DOI=10.1016/0378-1119(92)90006-b;
RA   Cousineau B., Cerpa C., Lefebvre J., Cedergren R.;
RT   "The sequence of the gene encoding elongation factor Tu from Chlamydia
RT   trachomatis compared with those of other organisms.";
RL   Gene 120:33-41(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-11.
RA   Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M.,
RA   Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G.,
RA   Pallini V.;
RL   Submitted (SEP-1994) to UniProtKB.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
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DR   EMBL; M74221; AAA62238.1; -; Genomic_DNA.
DR   EMBL; AM884176; CAP04014.1; -; Genomic_DNA.
DR   PIR; JC1420; JC1420.
DR   RefSeq; WP_009873724.1; NC_010287.1.
DR   RefSeq; YP_001654650.1; NC_010287.1.
DR   AlphaFoldDB; B0B7N8; -.
DR   SMR; B0B7N8; -.
DR   PRIDE; B0B7N8; -.
DR   EnsemblBacteria; CAP04014; CAP04014; CTL0574.
DR   KEGG; ctb:CTL0574; -.
DR   PATRIC; fig|471472.4.peg.615; -.
DR   HOGENOM; CLU_007265_0_0_0; -.
DR   OMA; EGDKEWG; -.
DR   Proteomes; UP000000795; 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; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
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; T_Tr_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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           2..394
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_1000095056"
FT   DOMAIN          10..204
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   CONFLICT        11
FT                   /note="P -> D (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17
FT                   /note="T -> A (in Ref. 1; AAA62238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="K -> R (in Ref. 1; AAA62238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="T -> P (in Ref. 1; AAA62238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="G -> C (in Ref. 1; AAA62238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255..259
FT                   /note="IVTGV -> LLLGL (in Ref. 1; AAA62238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265..269
FT                   /note="ELPEG -> NSQKV (in Ref. 1; AAA62238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="R -> L (in Ref. 1; AAA62238)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  43309 MW;  3F013074478170FD CRC64;
     MSKETFQRNK PHINIGTIGH VDHGKTTLTA AITRTLSGDG LADFRDYSSI DNTPEEKARG
     ITINASHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSATD GAMPQTKEHI
     LLARQVGVPY IVVFLNKIDM ISEEDAELVD LVEMELAELL EEKGYKGCPI IRGSALKALE
     GDAAYIEKVR ELMQAVDDNI PTPEREIDKP FLMPIEDVFS ISGRGTVVTG RIERGIVKVS
     DKVQLVGLRD TKETIVTGVE MFRKELPEGR AGENVGLLLR GIGKNDVERG MVVCLPNSVK
     PHTRFKCAVY VLQKEEGGRH KPFFTGYRPQ FFFRTTDVTG VVTLPEGVEM VMPGDNVEFE
     VQLISPVALE EGMRFAIREG GRTIGAGTIS KIIA
 
 
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