TETQ_PREIN
ID TETQ_PREIN Reviewed; 654 AA.
AC O05197;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tetracycline resistance protein TetQ;
DE Short=Tet(Q);
GN Name=tetQ; Synonyms=tet(Q);
OS Prevotella intermedia.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=28131;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PDRC-11;
RA Bueno L.B., Presnail J.K., Walker C.B.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51122.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U73497; AAB51122.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_063856408.1; NG_048271.1.
DR AlphaFoldDB; O05197; -.
DR SMR; O05197; -.
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..654
FT /note="Tetracycline resistance protein TetQ"
FT /id="PRO_0000091512"
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 654 AA; 74132 MW; 653CF3D193C23A1C CRC64;
MNIINLGILA HIDAGKTSVT ENLLFASGAT EKCGRVDNGD TITDSMDIEK RRGITVRAST
TSIIWNGVKC NIIDTPGHMD FIAEVERTFK MLDGAVLILS AKEGIQAQTK LLFNTLQKLQ
IPTIIFINKI DRDGVNLERL YLDIKTNLSQ DVLFMQTVVD GLVYPICSQT YIKEEYKEFV
CNHDDNILER YLADSEISPA DYWNTIIDLV AKAKVYPVLH GSAMFNIGIN ELLDAISSFI
LPPESVSNRL SAYLYKIEHD PKGHKRSFLK IIDGSLRLRD IVRINDSEKF IKIKNLKTIY
QGRKINVDEV GANDIAIVED MEDFRIGDYL GTKPCLIQGL SHQHPALKSS VRPDRSEERS
KVISALNTLW IEDPSLSFSI NSYSDELEIS LYGLTQKEII QTLLEERFSV KVHFDEIKTI
YKERPVKKVN KIIQIEVPPN PYWATIGLTL EPLPLGTGLQ IESDISYGYL NHSFQNAVFE
GIRMSCQSGL HGWEVTDLKV TFTQAEYYSP VSTPADFRQL TPYVFRLALQ QSGVDILEPM
LYFELQIPQA ASSKAITDLQ KMMSEIEDIS CNNEWCHIKG KVPYNTSKDY ASEVSSYTKG
LGVFMVKPCG YQITKGDYSD NIRMNEKDKI LFMFQKSNVI KIMERSGNFY KAIQ