LNRM_BACSU
ID LNRM_BACSU Reviewed; 396 AA.
AC P94441; Q796Z6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Linearmycin resistance permease protein LnrM {ECO:0000305};
GN Name=lnrM {ECO:0000303|PubMed:28461449};
GN Synonyms=bifM {ECO:0000312|EMBL:CAB12661.1}, yfiM;
GN OrderedLocusNames=BSU08320;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8973323; DOI=10.1016/s0378-1119(96)00495-7;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "The Bacillus subtilis chromosome region near 78 degrees contains the genes
RT encoding a new two-component system, three ABC transporters and a lipase.";
RL Gene 181:147-151(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION.
RX PubMed=26647299; DOI=10.1371/journal.pgen.1005722;
RA Stubbendieck R.M., Straight P.D.;
RT "Escape from lethal bacterial competition through coupled activation of
RT antibiotic resistance and a mobilized subpopulation.";
RL PLoS Genet. 11:E1005722-E1005722(2015).
RN [4]
RP FUNCTION, SUBUNIT, AND INDUCTION.
RX PubMed=28461449; DOI=10.1128/jb.00186-17;
RA Stubbendieck R.M., Straight P.D.;
RT "Linearmycins activate a two-component signaling system involved in
RT bacterial competition and biofilm morphology.";
RL J. Bacteriol. 199:E00186-E00186(2017).
CC -!- FUNCTION: Required for resistance to linearmycins, a family of
CC antibiotic-specialized metabolites produced by some streptomycetes
CC (PubMed:26647299, PubMed:28461449). Part of the ABC transporter complex
CC LnrLMN that probably facilitates linearmycin removal from the membrane.
CC Responsible for the translocation of the substrate across the membrane
CC (PubMed:28461449). Also mediates KinC-dependent biofilm morphology
CC (PubMed:28461449). {ECO:0000269|PubMed:26647299,
CC ECO:0000269|PubMed:28461449}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (LnrL) and
CC two transmembrane proteins (LnrM and LnrN).
CC {ECO:0000305|PubMed:28461449}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Induced in response to linearmycins and other polyenes via
CC the two-component regulatory system LnrJ/LnrK.
CC {ECO:0000269|PubMed:28461449}.
CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D78508; BAA11403.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12661.1; -; Genomic_DNA.
DR PIR; H69803; H69803.
DR RefSeq; NP_388713.1; NC_000964.3.
DR RefSeq; WP_003242483.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P94441; -.
DR SMR; P94441; -.
DR STRING; 224308.BSU08320; -.
DR TCDB; 3.A.1.105.19; the atp-binding cassette (abc) superfamily.
DR jPOST; P94441; -.
DR PaxDb; P94441; -.
DR PRIDE; P94441; -.
DR EnsemblBacteria; CAB12661; CAB12661; BSU_08320.
DR GeneID; 939210; -.
DR KEGG; bsu:BSU08320; -.
DR PATRIC; fig|224308.179.peg.899; -.
DR eggNOG; COG0842; Bacteria.
DR eggNOG; COG1511; Bacteria.
DR InParanoid; P94441; -.
DR OMA; KSIWIAW; -.
DR BioCyc; BSUB:BSU08320-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR000412; ABC_2_transport.
DR PROSITE; PS51012; ABC_TM2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..396
FT /note="Linearmycin resistance permease protein LnrM"
FT /id="PRO_0000360051"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 161..396
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ SEQUENCE 396 AA; 43114 MW; 8546B7582F948EAA CRC64;
MKKSIWIAWK DVKIRITDRK GFMMLILMPL ILTCILGAAL GSVVDGGSRI DDIKVGYIQS
DQSDTANMFT KDVLKKMKSI KVTKVGSKDK MKKLIDEKKI DVGIVIPNHW EAGKTSAVVN
AAPDQTLKSS IIETAASSFI EQYKAVKEAA SGSMDYISKT EAVKQGKLDP AQFAEKLAKT
LEKETGDKLT IAEKSVGSKA VTSFQYYSAA MLCMFMLFHI TVGAKSFLQE KDTETLARML
MTPAQKSVIL FGKWLGTYLF AIIQFFIFLI VTINVFGVDW GGNLLLVSVL GLSYAAAVSG
ISMLLASCIS DMKTADAIGG FGIQLLAVLG GSMLPLYQFP DVLQSVSKAV PNRWALDGFL
SLMEGGGWAD LQKPVLLFAA IGFCSLVIGI RRLHTR
