LNRN_BACSU
ID LNRN_BACSU Reviewed; 385 AA.
AC P94442; Q796Z5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Linearmycin resistance permease protein LnrN {ECO:0000305};
GN Name=lnrN {ECO:0000303|PubMed:28461449};
GN Synonyms=bifN {ECO:0000312|EMBL:CAB12662.1}, yfiN;
GN OrderedLocusNames=BSU08330;
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}.
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DR EMBL; D78508; BAA11404.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12662.1; -; Genomic_DNA.
DR PIR; A69804; A69804.
DR RefSeq; NP_388714.1; NC_000964.3.
DR RefSeq; WP_003243650.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P94442; -.
DR SMR; P94442; -.
DR STRING; 224308.BSU08330; -.
DR TCDB; 3.A.1.105.19; the atp-binding cassette (abc) superfamily.
DR PaxDb; P94442; -.
DR PRIDE; P94442; -.
DR EnsemblBacteria; CAB12662; CAB12662; BSU_08330.
DR GeneID; 939705; -.
DR KEGG; bsu:BSU08330; -.
DR PATRIC; fig|224308.179.peg.900; -.
DR eggNOG; COG0842; Bacteria.
DR InParanoid; P94442; -.
DR OMA; WVPVFAM; -.
DR PhylomeDB; P94442; -.
DR BioCyc; BSUB:BSU08330-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..385
FT /note="Linearmycin resistance permease protein LnrN"
FT /id="PRO_0000360052"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 163..382
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ SEQUENCE 385 AA; 42084 MW; 0E5A8C5B9BAF145E CRC64;
MKKILAICGI ELSLIFKKPQ NYLIMFAAPL LLTFVFGSML SGNDDKVRLA IVDQDDTILS
QHYIRQLKAH DDMYVFENMS ESKASEKLKQ KKIAGIIVIS RSFQTQLEKG KHPELIFRHG
PELSEAPMVK QYAESALATL NIQVTAAKTA SQTAGENWKA AYKTVFAKKH EDIVPAVTRQ
TLSDKKEGAE ASDTASRAAG FSILFVMLTM MGAAGTILEA RKNGVWSRLL TASVSRAEIG
AGYVLSFFVI GWIQFGILLL STHWLFGINW GNPAAVIVLV SLFLLTVVGI GLMIAANVRT
PEQQLAFGNL FVIATCMVSG MYWPIDIEPK FMQSIAEFLP QKWAMSGLTE IIANGARVTD
ILGICGILLA FAAITFAAGL KALRA
