ID   TLRC_STRFR              Reviewed;         548 AA.
AC   P25256;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Tylosin resistance ATP-binding protein TlrC;
GN   Name=tlrC;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1864505; DOI=10.1016/0378-1119(91)90533-h;
RA   Rosteck P.R. Jr., Reynolds P.A., Hershberger C.L.;
RT   "Homology between proteins controlling Streptomyces fradiae tylosin
RT   resistance and ATP-binding transport.";
RL   Gene 102:27-32(1991).
CC   -!- FUNCTION: Responsible for tylosin resistance, and is proposed to be a
CC       subunit of a multicomponent export system for the energy-dependent
CC       efflux of tylosin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; M57437; AAA26832.1; -; Genomic_DNA.
DR   PIR; JQ1142; JQ1142.
DR   RefSeq; WP_063856491.1; NG_048321.1.
DR   AlphaFoldDB; P25256; -.
DR   SMR; P25256; -.
DR   STRING; 1906.SFRA_29725; -.
DR   TCDB; 3.A.1.120.2; the atp-binding cassette (abc) superfamily.
DR   PRIDE; P25256; -.
DR   KEGG; ag:AAA26832; -.
DR   eggNOG; COG0488; Bacteria.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Repeat; Transport.
FT   CHAIN           1..548
FT                   /note="Tylosin resistance ATP-binding protein TlrC"
FT                   /id="PRO_0000093024"
FT   DOMAIN          9..265
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          347..547
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         387..394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   548 AA;  59130 MW;  1E085B54F7B8B171 CRC64;
     MRTSPSSQLS LHGVTKRYDD RVVLSQVSLA ISPGEKAGII GDNGAGKSTL LRLLAGEERP
     DAGEVTVIAP GGVGYLPQTL GLPPRATVQD AIDLAMTELR VLEAELRRTE AALAEAATDE
     ALQDALTAYA RLTEQYEVRD GYGADARVDA ALHGLGLPGL PRDRRLGTLS GGERSRLALA
     ATLASQPELL LLDEPTNDLD DRAVHWLEEH LSGHRGTVVT VTHDRVFLDR LTATVLEVDG
     RGVSRHGDGY AGYLAAKAAE RRRRQQQYDE WRAELDRNRR LAEANVARLD GIPRKMGKAA
     FGHGAFRARG RDHGAMSRVR NAKERVERLT ANPVAPPADR LSLTARIATA DGPGEAPAAE
     LDGVVVGSRL RVPKLRLGAA ERLLITGPNG AGKSTLLSVL AGELSPDAGA VSVPGRVGHL
     RQEETPWPAK LTVLEAFAHN RPGDRDEQAD RRLSLGLFEP EALRLRVGEL SYGQRRRIEL
     ARLVSEPVGL LLLDEPTNHL SPALVEELEE ALTGYGGALV LVTHDRRMRS RFTGSHLELR
     EGVVSGAR