TETS_LISMN
ID TETS_LISMN Reviewed; 641 AA.
AC Q48791;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Tetracycline resistance protein TetS;
DE Short=Tet(S);
GN Name=tetS; Synonyms=tet(S);
OS Listeria monocytogenes.
OG Plasmid pIP811.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BM4210;
RX PubMed=8370538; DOI=10.1016/0378-1119(93)90665-p;
RA Charpentier E., Gerbaud G., Courvalin P.;
RT "Characterization of a new class of tetracycline-resistance gene tet(S) in
RT Listeria monocytogenes BM4210.";
RL Gene 131:27-34(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}.
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DR EMBL; L09756; AAA25293.1; -; Genomic_DNA.
DR PIR; JN0800; JN0800.
DR RefSeq; WP_000691722.1; NG_048273.1.
DR AlphaFoldDB; Q48791; -.
DR SMR; Q48791; -.
DR GeneID; 66817191; -.
DR KEGG; ag:AAA25293; -.
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; Plasmid;
KW Protein biosynthesis.
FT CHAIN 1..641
FT /note="Tetracycline resistance protein TetS"
FT /id="PRO_0000091515"
FT DOMAIN 1..242
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; 73014 MW; EC534FD38FD54FC2 CRC64;
MKIINIGILA HVDAGKTTLT ESLLYSSGAI KELGSVDSGT TKTDTMFLER QRGITIQTAI
TSFQRENVKV NIVDTPGHMD FLADVYRSLS VLDGAILLIS AKDGVQSQTR ILFHALRKMN
IPIIFFINKI DQNGINLPDV YQDIKDKLSD DIIIKQTVNL NLKPYVIDYT EPEQWETVIV
GNDYLLEKYT IGKTLNIAEL EKEENERIQS CSLYPVYHGS AKNNIGIKQL IEVITSKLFS
PTQLNSDKLC GNVFKVEYSD DGQRLVYVRL YSGTLHLRDS VNISEKEKIK VTEMYTSING
ELRQIDKAEP GEIIILKNEL LKLNNVLGDK KRLPHREILE NPLPMLQTTI EPCKSVQREK
LLDALFEISD SDPLLQYYVD TVTHEIVLSF LGEVQMEVTC TLIQEKYHIE IETRKPTVIY
MERPLKKSEF TIDIEVPPNP FWASIGLSVT PLPLGSGIQY ESLVSLGYLN QSFQNAVMEG
IRYGCEQGLY GWKLTDCKIC FKYGLYYSPV STPADFRMLA PIVLEQAFRK SGTELLEPYL
SFEIYVPQEY LSRAYNDASK YCANILNTKL KGNEVILIGE IPARCIQEYR NSLTFFTNGR
SVCLTELKGY QVTNIKSAFQ PRRPNNRIDK VRHMFNKINL H