TETM_STAAU
ID TETM_STAAU Reviewed; 639 AA.
AC Q53770;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Tetracycline resistance protein TetM;
DE Short=TetA(M);
GN Name=tetM; Synonyms=tetA(M);
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2073121; DOI=10.1128/aac.34.11.2273;
RA Nesin M., Svec P., Lupski J.R., Godson G.N., Kreiswirth B., Projan S.J.;
RT "Cloning and nucleotide sequence of a chromosomally encoded tetracycline
RT resistance determinant, tetA(M), from a pathogenic, methicillin-resistant
RT strain of Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 34:2273-2276(1990).
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; M21136; AAA26678.1; -; Genomic_DNA.
DR PIR; A60633; A60633.
DR RefSeq; WP_063856108.1; NG_048214.1.
DR AlphaFoldDB; Q53770; -.
DR SMR; Q53770; -.
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 3: Inferred from homology;
KW Antibiotic resistance; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..639
FT /note="Tetracycline resistance protein TetM"
FT /id="PRO_0000091500"
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; 72639 MW; 66470062A673BE1F CRC64;
MKIINIGVLA HVDAGKTTLT ESLLYNSGAI TELGSVDKGT TRTDNTLLER QRGITIQTGI
TSFQWENTKV NIIDTPGHMD FLAEVYRSLS VLDGAILLIS AKDFVQAQTR ILFHALRKMG
IPTIFFINKI DQNGIDLSTV YQDIKEKLSA EIVIKQKVEL YPNMCVTNFT 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 STPADFRMLT PIVLEQAFRK AGTELLEPYL
SFKVYAPQEY LSRAYNDAPK YCANIVNTQL KNNEVIIIGE IPARCIQDYR NDLTFFTNGL
SVCLAELKGY QVTTGEPVCQ TRRLNSRIDK VRYMFNKIT