OTRA_STRRM
ID OTRA_STRRM Reviewed; 663 AA.
AC Q55002;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Oxytetracycline resistance protein;
GN Name=otrA;
OS Streptomyces rimosus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1927;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=15883R;
RX PubMed=1809836; DOI=10.1111/j.1365-2958.1991.tb01852.x;
RA Doyle D., McDowall K.J., Butler M.J., Hunter I.S.;
RT "Characterization of an oxytetracycline-resistance gene, otrA, of
RT Streptomyces rimosus.";
RL Mol. Microbiol. 5:2923-2933(1991).
CC -!- FUNCTION: Abolishes the inhibitory effect of oxytetracycline 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; X53401; CAA37477.1; -; Genomic_DNA.
DR PIR; S18572; S18572.
DR RefSeq; WP_063854497.1; NG_048026.1.
DR AlphaFoldDB; Q55002; -.
DR SMR; Q55002; -.
DR KEGG; ag:CAA37477; -.
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; 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; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
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..663
FT /note="Oxytetracycline resistance protein"
FT /id="PRO_0000091517"
FT DOMAIN 1..252
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 663 AA; 71786 MW; FEB03DE38856194D CRC64;
MNKLNLGILA HVDAGKTSLT ERLLHRTGVI DEVGSVDAGT TTTDSMELER QRGITIRSAV
ATFVLDDLKV NLIDTPGHSD FISEVERALG VLDGAVLVVS AVEGVQPQTR ILMRTLRRLG
IPTLVFVNKI DRGGARPDGV LREIRDRLTP AAVALSAVAD AGTPRARAIA LGPDTDPDFA
VRVGELLADH DDAFLTAYLD EEHVLTEKEY AEELAAQTAR GLVHPVYFGS ALTGEGLDHL
VHGIRELLPS VHASQDAPLR ATVFKVDRGA RGEAVAYLRL VSGTLGTRDS VTLHRVDHTG
RVTEHAGRIT ALRVFEHGSA TSETRATAGD IAQAWGLKDV RVGDRAGHLD GPPPRNFFAP
PSLETVIRPE RPEEAGRLHA ALRMLDEQDP SIDLRQDEEN AAGAVVRLYG EVQKEILGST
LAESFGVRVR FDPTRTVCIE KPVGTGEALI ELDTRTHNYF WGAPWVCASD RPSPARAITF
RLAVELGSLP LAFHKAIEET VHTTLRHGLY GWQVTDCAVT LTRTGVRSPV SAADDFRKAN
ARLVLMDALG RAGTEVHEPV SSFELEVPAA RLSPVLAKLA ELGATPGVPT AEGDVFRLEG
TMPTSLVHDF NQRVPGLTQG EGVFLAEHRG YRPAVGQPPV RPRPEGPNPL NRDEYILHVL
KRV