TETM_UREUR
ID TETM_UREUR Reviewed; 639 AA.
AC P09757;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Tetracycline resistance protein TetM;
GN Name=tetM;
OS Ureaplasma urealyticum (Ureaplasma urealyticum biotype 2).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=2130;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3344217; DOI=10.1093/nar/16.3.1216;
RA Sanchez-Pescador R., Brown J.T., Roberts M., Urdea M.S.;
RT "The nucleotide sequence of the tetracycline resistance determinant tetM
RT from Ureaplasma urealyticum.";
RL Nucleic Acids Res. 16:1216-1217(1988).
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; U08812; AAA73978.1; -; Unassigned_DNA.
DR PIR; S03268; S03268.
DR RefSeq; WP_063856110.1; NG_048216.1.
DR AlphaFoldDB; P09757; -.
DR SMR; P09757; -.
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_0000091503"
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; 72599 MW; A1497055BB182B3A 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 KLLPQRKRIE NPHPLLQITV EPSKPEQREM
LLDALLEISD SDPLLRYYVD STTHEIILSF LGKVQMEVIS ALLQEKYHVE IELKEPTVIY
MERPLKNAEY TIHIEVPPNP FWASIGLSVS PLPLGSGMQY ESSVSLGYLN QSFQNAVMEG
IRYGCEQGLY GWNVTECKIC FKYGLYYSPV STPADFRMLA PIVLEQVLKK AGTELLEPYL
SFKIYAPQEY LSRAYNDAPK YCANIVDTQL KNNEVILSGE IPARCIQEYR SDLTFFTNGR
SVCLTELKGY HVTTGEPVCQ PRRPNSRIDK VRYMFNKIT