GenomeNet

Database: UniProt
Entry: Q48712
LinkDB: Q48712
Original site: Q48712 
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   27-MAR-2024, entry version 101.
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; Bacillota; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   CDD; cd03690; Tet_II; 1.
DR   CDD; cd16258; Tet_III; 1.
DR   CDD; cd01684; Tet_like_IV; 1.
DR   CDD; cd04168; TetM_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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   PRINTS; PR01037; TCRTETOQM.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 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
//
DBGET integrated database retrieval system