ID   TETQ_BACT4              Reviewed;         641 AA.
AC   Q00937;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Tetracycline resistance protein TetQ;
DE   AltName: Full=TetA(Q)1;
GN   Name=tetQ; Synonyms=tet(Q);
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DOT;
RX   PubMed=1339256; DOI=10.1128/aac.36.5.1005;
RA   Nikolich M.P., Shoemaker N.B., Salyers A.A.;
RT   "A Bacteroides tetracycline resistance gene represents a new class of
RT   ribosome protection tetracycline resistance.";
RL   Antimicrob. Agents Chemother. 36:1005-1012(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 601-641.
RX   PubMed=1569023; DOI=10.1128/jb.174.9.2935-2942.1992;
RA   Stevens A.M., Sanders J.M., Shoemaker N.B., Salyers A.A.;
RT   "Genes involved in production of plasmidlike forms by a Bacteroides
RT   conjugal chromosomal element share amino acid homology with two-component
RT   regulatory systems.";
RL   J. Bacteriol. 174:2935-2942(1992).
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; X58717; CAA41552.1; -; Genomic_DNA.
DR   EMBL; M81439; AAA22919.1; -; Genomic_DNA.
DR   PIR; S23757; S23757.
DR   RefSeq; WP_004293868.1; NZ_JADPBE010000075.1.
DR   AlphaFoldDB; Q00937; -.
DR   SMR; Q00937; -.
DR   GeneID; 45365338; -.
DR   GeneID; 66339826; -.
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..641
FT                   /note="Tetracycline resistance protein TetQ"
FT                   /id="PRO_0000091511"
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   641 AA;  72156 MW;  3402C316627315D5 CRC64;
     MNIINLGILA HIDAGKTSVT ENLLFASGAT EKCGCVDNGD TITDSMDIEK RRGITVRAST
     TSIIWNGVKC NIIDTPGHMD FIAEVERTFK MLDGAVLILS AKEGIQAQTK LLFNTLQKLQ
     IPTIIFINKI DRAGVNLERL YLDIKANLSQ DVLFMQNVVD GSVYPVCSQT YIKEEYKEFV
     CNHDDNILER YLADSEISPA DYWNTIIALV AKAKVYPVLH GSAMFNIGIN ELLDAITSFI
     LPPASVSNRL SSYLYKIEHD PKGHKRSFLK IIDGSLRLRD VVRINDSEKF IKIKNLKTIN
     QGREINVDEV GANDIAIVED MDDFRIGNYL GAEPCLIQGL SHQHPALKSS VRPDRPEERS
     KVISALNTLW IEDPSLSFSI NSYSDELEIS LYGLTQKEII QTLLEERFSV KVHFDEIKTI
     YKERPVKKVN KIIQIEVPPN PYWATIGLTL EPLPLGTGLQ IESDISYGYL NHSFQNAVFE
     GIRMSCQSGL HGWEVTDLKV TFTQAEYYSP VSTPADFRQL TPYVFRLALQ QSGVDILEPM
     LYFELQIPQA ASSKAITDLQ KMMSEIEDIS CNNEWCHIKG KVPLNTSKDY ASEVSSYTKG
     LGIFMVKPCG YQITKGGYSD NIRMNEKDKL LFMFQKSMSS K