TETO_CAMCO
ID TETO_CAMCO Reviewed; 639 AA.
AC P23835;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Tetracycline resistance protein TetO;
DE Short=Tet(O);
GN Name=tetO; Synonyms=tet(O);
OS Campylobacter coli.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sougakoff W., Papadopoulou B., Nordmann P., Courvalin P.;
RT "Nucleotide sequence and distribution of gene tetO encoding tetracycline
RT resistance in Campylobacter coli.";
RL FEMS Microbiol. Lett. 44:153-159(1987).
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. TetM/TetO
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR PIR; S06388; S06388.
DR AlphaFoldDB; P23835; -.
DR SMR; P23835; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03711; Tet_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR035650; Tet_C.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
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 Antibiotic resistance; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..639
FT /note="Tetracycline resistance protein TetO"
FT /id="PRO_0000091504"
FT DOMAIN 1..244
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 639 AA; 72373 MW; 568C968E6DA9EA34 CRC64;
MKIINLGILA HVDAGKTTLT ESLLYTSGAI AEPGSVDKGT TRTDTINLER QRGITIQTAV
TSFQWEDVKV NIIDTPGHMD FLAEVYRSLS VLDGAVLLVS AKDGIQAQTR ILFHALQIMK
IPTIFFINKI DQEGIDLPMV YQEMKAKLSS EIIVKQKVGQ HPHINVTDND DMEQWDAVIM
GNDELLEKYM SGKPFKMSEL EQEENRRFQN GTLFPVYHGS AKNNLGIRQL IEVIASKFYS
STPEGQSELC GQVFKIEYSE KRRRFVYVRI YSGTLHLRDV IRISEKEKIK ITEMCVPTNG
ELYSSDTACS GDIVILPNDV LQLNSILGNE ILLPQRKFIE NPLPMLQTTI AVKKSEQREI
LLGALTEISD GDPLLKYYVD TTTHEIILSF LGNVQMEVIC AILEEKYHVE AEIKEPTVIY
MERPLRKAEY TIHIEVPPNP FWASVGLSIE PLLLGSGVQY ESRVSLGYLN QSFQNAVMEG
VLYGCEQGLY GWKVTDCKIC FEYGLYYSPV STPADFRLLS PIVLEQALKK AGTELLEPYL
HFEIYAPQEY LSRAYHDAPR YCADIVSTQI KNDEVILKGE IPARCIQEYR NDLTNFTNGQ
GVCLTELKGY QPAIGKFICQ PRRPNSRIDK VRHMFHKLA