TETM_NEIME
ID TETM_NEIME Reviewed; 639 AA.
AC Q51238;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tetracycline resistance protein TetM;
DE Short=Tet(M);
GN Name=tetM; Synonyms=tet(M);
OS Neisseria meningitidis.
OG Plasmid.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=23905;
RX PubMed=7730215; DOI=10.1093/jac/34.6.1015;
RA Gascoyne-Binzi D.M., Heritage J., Hawkey P.M., Sprott M.S.;
RT "Characterisation of a tet(M)-carrying plasmid from Neisseria
RT meningitidis.";
RL J. Antimicrob. Chemother. 34:1015-1023(1994).
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; X75073; CAA52967.1; -; Genomic_DNA.
DR PIR; S37283; S37283.
DR RefSeq; WP_063856109.1; NG_048215.1.
DR AlphaFoldDB; Q51238; -.
DR SMR; Q51238; -.
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; Plasmid;
KW Protein biosynthesis.
FT CHAIN 1..639
FT /note="Tetracycline resistance protein TetM"
FT /id="PRO_0000091498"
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; 72603 MW; 1D641087E280A83D CRC64;
MKIINIGVLA HVDAGKTTLT ESLLYNSGAI TELGSVDKGT TRTDNTLLER QRGITIQTGI
TSFQWENTKV NIIDTPGHMD FLAEVYRSLS VLDGAILLIS AKDGVQAQTR ILFHALRKMG
IPTIFFINKI DQNGIDLSTV YQDIKEKLSA EIVIKQKVEL YPNMCVTNFT ESEQWDTVIE
GNDDLLEKYM SGKSLEALEL EQEESIRFHN CSLFPVYHGS AKNNIGIDNL IEVITNKFYS
STHRGPSELC GNVFKIEYTK KRQRLAYIRL YSGVLHLRDS VRVSEKEKIK VTEMYTSING
ELCKIDRAYS GEIVILQNEF LKLNSVLGDT KLLPQRKKIE NPHPLLRTTV EPSKPEQREM
LLDALLEISD SDPLLRYYVD STTHEIILSF LGKVQMEVIS ALLQEKYHVE IELKEPTVIY
MERPLKNAEY TIHIEVPPNP FWASIGLSVS PLPLGSGMQY ESSVSLGYLN QSFQNAVMEG
IRYGCEQGLY GWNVTDCKIC FKYGLYYSPV STPADFRMLA PIVLEQVLKK AGTELLEPYL
SFKIYTPQEY LSRAYNDAPK YCANIVDTQL KNNEVILSGE IPARCIQEYR SDLTFFTNGR
SVCLTELKGY HVTTGEPVCQ PRRPNSRIDK VRYMFNKIT