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 27-MAR-2024, entry version 128.
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; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; 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 AlphaFoldDB; P11545; -.
DR SMR; P11545; -.
DR STRING; 100226.gene:17765747; -.
DR PATRIC; fig|100226.15.peg.8184; -.
DR HOGENOM; CLU_000960_28_2_11; -.
DR InParanoid; P11545; -.
DR OrthoDB; 9781469at2; -.
DR PhylomeDB; P11545; -.
DR Proteomes; UP000001973; Plasmid SCP1.
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 CDD; cd17321; MFS_MMR_MDR_like; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 1.20.1720.10; Multidrug resistance protein D; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR42718; MAJOR FACILITATOR SUPERFAMILY MULTIDRUG TRANSPORTER MFSC; 1.
DR PANTHER; PTHR42718:SF40; METHYLENOMYCIN A RESISTANCE PROTEIN; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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
//
