TETM_STRLI
ID TETM_STRLI Reviewed; 639 AA.
AC Q02652;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tetracycline resistance protein TetM;
GN Name=tetM; Synonyms=tet;
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=66 / 1326;
RX PubMed=1510403; DOI=10.1128/aac.36.5.1119;
RA Dittrich W., Schrempf H.;
RT "The unstable tetracycline resistance gene of Streptomyces lividans 1326
RT encodes a putative protein with similarities to translational elongation
RT factors and Tet(M) and Tet(O) proteins.";
RL Antimicrob. Agents Chemother. 36:1119-1124(1992).
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; M74049; AAA26830.1; -; Genomic_DNA.
DR PIR; A48900; A48900.
DR AlphaFoldDB; Q02652; -.
DR SMR; Q02652; -.
DR KEGG; ag:AAA26830; -.
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; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
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; 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; 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_0000091501"
FT DOMAIN 1..247
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 247..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 67172 MW; 947FEBEA55BD5E1A CRC64;
MRTLNIGILA HVDAGKTSLT ERLLFDHGAV DRLGSVDAGD TRTVDGGIER RRGITIRSAV
AAFTVGDTRV NLIDTPGHSD FVAEVERALE VLDGAVLLLS AVEGVQARTR VLMRALRRLR
LPTIVFVNKI DRAGARTDGL LGDVRRLLTP HVAPLTEVAD AGTPRARVTR RPPDGRTAEA
LAEVDTEVLA ALVDGPEPTG EDVARALAAR TADGSFHPLY HGSALGGQGV AELVEGLLGL
IPAATPGTSG GTSGGTEPRG TVFAVRPGPA GERTAYLRLY GGEVHPRRRL TFLRRESDGR
TTEVSGRVTR LDVVGGDATL TAGNIAALTV PGGLRVGDRL GGPTDRAPQF APPTLQTLVR
ARHPEQAAPL RSALLALADQ DPLLHARPAA SGATALLLYG EVQMEVLAAT LAEDFGIEAE
FTPGRVRFLE RPAGTDEAAE EMPWLDRTRY FATIGLRVEP GPRGSGGAFG YETELGALPR
AFHQAVEETV HDTLRTGLTG AAVTDYRVTL IRSGFSSPLS TAADFRGLTP LVLRRALARA
GTVLHEPYQA FEAEVPADTL AAVTALLASL GADFTGTTGG DPAWIVTGEL PARRVREAEL
RLPGLTHGEA VWSSRPCEDR PLKAGNSGPG TGVGGHSGE