ID   TET1_ENTFL              Reviewed;         639 AA.
AC   Q47810;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Tetracycline resistance protein TetM from transposon TnFO1;
DE            Short=Tet(M);
GN   Name=tetM; Synonyms=tet(M);
OS   Enterococcus faecalis (Streptococcus faecalis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FO1; TRANSPOSON=TnFO1;
RA   Perreten V., Kolloeffel B., Teuber M.;
RT   "Conjugal transfer of Tn916-like transposon TnFO1 from Enterococcus
RT   faecalis FO1 to several Gram-positive bacteria.";
RL   Syst. Appl. Microbiol. 20:27-38(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Perreten V.;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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; X92947; CAA63530.2; -; Genomic_DNA.
DR   RefSeq; WP_000691749.1; NZ_WVTJ01000018.1.
DR   PDB; 3J25; EM; 7.20 A; A=2-639.
DR   PDBsum; 3J25; -.
DR   AlphaFoldDB; Q47810; -.
DR   SMR; Q47810; -.
DR   IntAct; Q47810; 1.
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; 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   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Transposable element.
FT   CHAIN           1..639
FT                   /note="Tetracycline resistance protein TetM from transposon
FT                   TnFO1"
FT                   /id="PRO_0000091497"
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   639 AA;  72491 MW;  D5299DCA60467C3D CRC64;
     MKIINIGVLA HVDAGKTTLT ESLLYNSGAI TELGSVDKGT TRTDNTLLER QRGITIQTGI
     TSFQWENTKV NIIDTPGHMD FLAEVYRSLS VLDGAILLIS AKDGVQAQTR ILFHALRKMG
     IPTIFFINKI DQNGIDLSTV YQDIKEKLSA EIVIKQKVEL YPNVCVTNFT ESEQWDTVIE
     GNDDLLEKYM SGKSLEALEL EQEESIRFQN CSLFPLYHGS AKSNIGIDNL IEVITNKFYS
     STHRGPSELC GNVFKIEYTK KRQRLAYIRL YSGVLHLRDS VRVSEKEKIK VTEMYTSING
     ELCKIDRAYS GEIVILQNEF LKLNSVLGDT KLLPQRKKIE NPHPLLQTTV EPSKPEQREM
     LLDALLEISD SDPLLRYYVD STTHEIILSF LGKVQMEVIS ALLQEKYHVE IELKEPTVIY
     MERPLKNAEY TIHIEVPPNP FWASIGLSVS PLPLGSGMQY ESSVSLGYLN QSFQNAVMEG
     IRYGCEQGLY GWNVTDCKIC FKYGLYYSPV STPADFRMLA PIVLEQVLKK AGTELLEPYL
     SFKIYAPQEY LSRAYNDAPK YCANIVDTQL KNNEVILSGE IPARCIQEYR SDLTFFTNGR
     SVCLTELKGY HVTTGEPVCQ PRRPNSRIDK VRYMFNKIT