ID   TET9_ENTFL              Reviewed;         639 AA.
AC   P21598;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Tetracycline resistance protein TetM from transposon Tn916;
DE            Short=TetM(916);
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   TRANSPOSON=Tn916;
RX   PubMed=2172929; DOI=10.1093/nar/18.20.6137;
RA   Burdett V.;
RT   "Nucleotide sequence of the tet(M) gene of Tn916.";
RL   Nucleic Acids Res. 18:6137-6137(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12.
RX   PubMed=1993661; DOI=10.1016/s0021-9258(18)49928-0;
RA   Burdett V.;
RT   "Purification and characterization of Tet(M), a protein that renders
RT   ribosomes resistant to tetracycline.";
RL   J. Biol. Chem. 266:2872-2877(1991).
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; X56353; CAA39796.1; -; Genomic_DNA.
DR   PIR; S13142; S13142.
DR   RefSeq; WP_063856107.1; NG_048211.1.
DR   PDB; 3J9Y; EM; 3.90 A; w=1-639.
DR   PDB; 5KCS; EM; 3.90 A; 1w=1-639.
DR   PDBsum; 3J9Y; -.
DR   PDBsum; 5KCS; -.
DR   AlphaFoldDB; P21598; -.
DR   SMR; P21598; -.
DR   IntAct; P21598; 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; Direct protein sequencing;
KW   GTP-binding; Nucleotide-binding; Protein biosynthesis;
KW   Transposable element.
FT   CHAIN           1..639
FT                   /note="Tetracycline resistance protein TetM from transposon
FT                   Tn916"
FT                   /id="PRO_0000091496"
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;  72464 MW;  B2315A37B53B18FB 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 IEITEPTVIY
     MERPLKNAEY TIHIEVPPNP FWASIGLSVS PLPLGSGMQY ESSVSLGYLN QSFQNAVMEG
     IRYGCEQGLY GWNVTDCKIC FKYGLYYSPV STPADFRMLA PIVLEQVLKK AGTELLEPYL
     SFKIYAPQEY LSRAYNDAPK YCANIVDTQL KNNEVILSGE IPARCIQEYR SDLTFFTNGR
     SVCLTELKGY HVTTGEPVCQ PRRPNSRIDK VRYMFNKIT