TETS_LACLL
ID TETS_LACLL Reviewed; 646 AA.
AC Q48712;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
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 Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG Plasmid pK214.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K214;
RX PubMed=9349809; DOI=10.1038/39767;
RA Perreten V., Schwarz F., Cresta L., Boeglin M., Dasen G., Teuber M.;
RT "Antibiotic resistance spread in food.";
RL Nature 389:801-802(1997).
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; X92946; CAA63528.1; -; Genomic_DNA.
DR RefSeq; YP_001429542.1; NC_009751.1.
DR AlphaFoldDB; Q48712; -.
DR SMR; Q48712; -.
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..646
FT /note="Tetracycline resistance protein TetS"
FT /id="PRO_0000091514"
FT DOMAIN 6..247
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 79..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 646 AA; 73712 MW; 1F3513BA2F644B6B CRC64;
MEEIKLKIIN IGILAHVDAG KTTLTESLLY SSGRIKELGS VDSGTTKTDT MFLERQRGIT
IQTAITSFQR ENVKVNIVDT PGHMDFLADV YRSLSVLDGA ILLISAKDGV QSQTRILFHA
LRKMNIPIIF FINKIDQNGI NLPDVYQDIK DKLSDDIIIK QTVNLNLKPY VIDYTEPEQW
ETVIVGNDYL LEKYTIGKTL NIAELEKEEN ERIQSCSLYP VYHGSAKNNI GIKQLIEVIT
SKLFSPTQLN SDKLCGNVFK VEYSDDGQRL VYVRLYSGTL HLRDSVNISE KEKIKVTEMY
TSINGELRQI DKAEPGEIII LKNELLKLNN VLGDKKRLPH REILENPLPM LQTTIEPCKS
VQREKLLDAL FEISDSDPLL QYYVDTVTHE IVLSFLGEVQ MEVTCTLIQE KYHIEIETRK
PTVIYMERPL KKSEFTIDIE VPPNPFWASI GLSVTPLPLG SGIQYESLVS LGYLNQSFQN
AVMEGIRYGC EQGLYGWKLT DCKICFKYGL YYSPVSTPAD FRMLAPIVLE QAFRKSGTEL
LEPYLSFEIY VPQEYLSRAY NDASKYCANI LNTKLKGNEV ILIGEIPARC IQEYRNSLTF
FTNGRSVCLT ELKGYQVTNI KSAFQPRRPN NRIDKVRHMF NKINLH
