TETQ_BACFG
ID TETQ_BACFG Reviewed; 641 AA.
AC Q08425;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tetracycline resistance protein TetQ;
DE AltName: Full=TetA(Q)2;
GN Name=tetQ; Synonyms=tet(Q);
OS Bacteroides fragilis.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=817;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1126;
RX PubMed=7916585; DOI=10.1128/aac.37.9.2037;
RA Lepine G., Lacroix J.-M., Walker C.B., Progulske-Fox A.;
RT "Sequencing of a tet(Q) gene isolated from Bacteroides fragilis 1126.";
RL Antimicrob. Agents Chemother. 37:2037-2041(1993).
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=CAA79727.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z21523; CAA79728.1; -; Genomic_DNA.
DR EMBL; Z21523; CAA79727.1; ALT_INIT; Genomic_DNA.
DR PIR; I40188; I40188.
DR RefSeq; WP_002560998.1; NZ_SRKB01000002.1.
DR AlphaFoldDB; Q08425; -.
DR SMR; Q08425; -.
DR GeneID; 66377474; -.
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_0000091510"
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; 72523 MW; 4754576D8FDD5347 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
QGREINVDEV 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 KVPLNTSKDY ASEVSSYTKG
LGVFMVKPCG YQITKGDYSD NIRMNEKDKL LFMFQKSMSS K