ID TETO_STRMG Reviewed; 639 AA.
AC P20174;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Tetracycline resistance protein TetO;
DE Short=Tet(O);
GN Name=tetO; Synonyms=tet(O);
OS Streptococcus mutans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1309;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DL5;
RX PubMed=2841293; DOI=10.1128/jb.170.8.3618-3626.1988;
RA Leblanc D.J., Lee L.N., Titmas B.M., Smith C.J., Tenover F.C.;
RT "Nucleotide sequence analysis of tetracycline resistance gene tetO from
RT Streptococcus mutans DL5.";
RL J. Bacteriol. 170:3618-3626(1988).
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 EMBL; M20925; AAA26679.1; -; Genomic_DNA.
DR PIR; A31098; A31098.
DR RefSeq; WP_044666383.1; NG_048254.1.
DR AlphaFoldDB; P20174; -.
DR SMR; P20174; -.
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 CDD; cd03690; Tet_II; 1.
DR CDD; cd16258; Tet_III; 1.
DR CDD; cd01684; Tet_like_IV; 1.
DR CDD; cd04168; TetM_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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 PRINTS; PR01037; TCRTETOQM.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 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_0000091506"
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; 72470 MW; 68403C1E02007C07 CRC64;
MKIINLGILA HVDAGKTTLT ESLLYTSGAI AEPGSVDKGT TRTDTMNLER QRGITIQTAV
TSFQWEDVKV NIIDTPGHMD FLAEVYRSLS VLDGAVLLVS AKDGIQAQTR ILFHALQTMK
IPTIFFINKI DQEGIDLPMV YREMKAKLSS EIIVKQKVGQ HPHINVTDND DMEQWDTVIM
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 PLPIGSGVQY ESRVSLGYLN QSFQNAVMEG
VLYGCEQGLY GWKVTDCKIC FEYGLYYSPV STPADFRLLS PIVLEQALKK AGTELLEPYL
HFEIYAPQEY LSRAYHDAPR YCADIVSTQI KNDEVILKGE IPARCIQEYR NDLTYFTNGQ
GVCLTELKGY QPAIGKFICQ PRRPNSRIDK VRHMFHKLA
//
