TETQ_PRERU
ID TETQ_PRERU Reviewed; 641 AA.
AC Q52360;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Tetracycline resistance protein TetQ;
DE Short=Tet(Q);
GN Name=tetQ;
OS Prevotella ruminicola (Bacteroides ruminicola).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=223;
RX PubMed=7944364; DOI=10.1128/aem.60.9.3255-3260.1994;
RA Nikolich M.P., Hong G., Shoemaker N.B., Salyers A.A.;
RT "Evidence for natural horizontal transfer of tetQ between bacteria that
RT normally colonize humans and bacteria that normally colonize livestock.";
RL Appl. Environ. Microbiol. 60:3255-3260(1994).
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; L33696; AAA62400.1; -; Genomic_DNA.
DR RefSeq; WP_063856407.1; NZ_FNUV01000012.1.
DR AlphaFoldDB; Q52360; -.
DR SMR; Q52360; -.
DR KEGG; ag:AAA62400; -.
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_0000091513"
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; 72270 MW; 812330D9D7593D38 CRC64;
MNIINLGILA HIDAGKTSVT ENLLFASGAT EKCGRVDNGD TITDSMDIEK RRGITVRAST
TSIIWNGVKC NIIDTPGHMD FIAEVERTFK MLDGAVLILS AKEGIQAQTK LLFSTLQKLQ
IPTIIFINKI DRAGVNLERL YMDIKTNLSQ DVLFMQTVVD GSVYPVCSQT YIKEEYKEFV
CNHDDDILER YLADSEISPA DYWNTIIALV AKAKVYPVLH GSAMFNIGIN ELLDAITSFI
LPPASVSNRL SAYLYKIEHD PKGHKRSFLK IIDGSLRLRD VVRINDSEKF IKIKNLKTIY
QGREINVDEV GANDIAIVED IEDFRIGDYL GAKPCLIQGL SHQHPALKCS VRPNKPEERS
KVISALNTLW IEDPSLSFSI NSYSDELEIS LYGLTQKEII QTLLEERFSV KVHFDEIKTI
YKERPIKKVN KIIQIEVPPN PYWATIGLTL EPLPLGAGLQ IESDISYGYL NHSFQNAVFE
GIRMSCQSGL HGWEVTDLKV TFTQAEYYSP VSTPADFRQL TPYVFRLALQ QSGVDILEPM
LCFELQIPQV ASSKAITDLQ KMMSEIEDIS CNNEWCHIKG KVPLNTSKDY ASEVSSYTKG
LGIFMVKPCG YQITKDGYSD NIRMNEKDKL LFMFQKSMSL K