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MMR_STRCO
ID   MMR_STRCO               Reviewed;         475 AA.
AC   P11545;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Methylenomycin A resistance protein;
DE   AltName: Full=MMR peptide;
GN   Name=mmr; OrderedLocusNames=SCP1.237c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OG   Plasmid SCP1.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=2828187; DOI=10.1016/0378-1119(87)90378-7;
RA   Neal R.J., Chater K.F.;
RT   "Nucleotide sequence analysis reveals similarities between proteins
RT   determining methylenomycin A resistance in Streptomyces and tetracycline
RT   resistance in eubacteria.";
RL   Gene 58:229-241(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Bruton C.J., Wietzorrek A., Hartley N., Woodburn L., Chater K.F.;
RT   "Genes involved in methylenomycin biosynthesis from plasmid SCP1 of
RT   Streptomyces coelicolor A3(2).";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Resistance to the epoxide antibiotic methylenomycin A;
CC       probably by mediating its efflux.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; M18263; AAA98341.1; -; Genomic_DNA.
DR   EMBL; AJ276673; CAB82871.1; -; Genomic_DNA.
DR   EMBL; AL589148; CAC36763.1; -; Genomic_DNA.
DR   PIR; B29606; B29606.
DR   RefSeq; NP_639847.1; NC_003903.1.
DR   RefSeq; WP_011039539.1; NC_003903.1.
DR   AlphaFoldDB; P11545; -.
DR   SMR; P11545; -.
DR   GeneID; 1095320; -.
DR   KEGG; sco:SCP1.237c; -.
DR   PATRIC; fig|100226.15.peg.8184; -.
DR   HOGENOM; CLU_000960_28_2_11; -.
DR   InParanoid; P11545; -.
DR   OMA; WTIFAGM; -.
DR   PhylomeDB; P11545; -.
DR   Proteomes; UP000001973; Plasmid SCP1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Membrane; Plasmid;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..475
FT                   /note="Methylenomycin A resistance protein"
FT                   /id="PRO_0000173365"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   475 AA;  49239 MW;  CF35F49BA9535102 CRC64;
     MTTVRTGGAQ TAEVPAGGRR DVPSGVKITA LATGFVMATL DVTVVNVAGA TIQESLDTTL
     TQLTWIVDGY VLTFASLLML AGGLANRIGA KTVYLWGMGV FFLASLACAL APTAETLIAA
     RLVQGAGAAL FMPSSLSLLV FSFPEKRQRT RMLGLWSAIV ATSSGLGPTV GGLMVSAFGW
     ESIFLLNLPI GAIGMAMTYR YIAATESRAT RLAVPGHLLW IVALAAVSFA LIEGPQLGWT
     AGPVLTAYAV AVTAAALLAL REHRVTNPVM PWQLFRGPGF TGANLVGFLF NFALFGSTFM
     LGLYFQHARG ATPFQAGLEL LPMTIFFPVA NIVYARISAR FSNGTLLTAF LLLAGAASLS
     MVTITASTPY WVVAVAVGVA NIGAGIISPG MTAALVDAAG PENANVAGSV LNANRQIGSL
     VGIAAMGVVL HSTSDWDHGA AISFLAVGLA YLLGGLSAWR LIARPERRSA VTAAT
 
 
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