ID LNRJ_BACSU Reviewed; 400 AA.
AC P94438; Q796Z9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Sensor histidine kinase LnrJ {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P13799};
GN Name=lnrJ {ECO:0000303|PubMed:28461449};
GN Synonyms=linJ {ECO:0000312|EMBL:CAB12658.1}, yfiJ;
GN OrderedLocusNames=BSU08290;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; 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=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA Fujita Y.;
RT "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT regulatory systems.";
RL J. Bacteriol. 183:7365-7370(2001).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-201.
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 [5]
RP FUNCTION.
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). Member of the two-component
CC regulatory system LnrJ/LnrK, which induces expression of the LnrLMN ABC
CC transporter in response to linearmycins and other polyenes
CC (PubMed:11717295, PubMed:26647299, PubMed:28461449). Acts as a specific
CC sensor for linearmycin, either directly through binding or indirectly
CC through membrane perturbation. Probably activates LnrK by
CC phosphorylation (PubMed:28461449). May also promote biofilm formation
CC (PubMed:28461449). {ECO:0000269|PubMed:11717295,
CC ECO:0000269|PubMed:26647299, ECO:0000269|PubMed:28461449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P13799};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P13799}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant does not show any observable
CC phenotype. {ECO:0000269|PubMed:26647299}.
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DR EMBL; D78508; BAA11400.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12658.1; -; Genomic_DNA.
DR PIR; JC5358; JC5358.
DR RefSeq; NP_388710.1; NC_000964.3.
DR RefSeq; WP_009966811.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P94438; -.
DR SMR; P94438; -.
DR STRING; 224308.BSU08290; -.
DR PaxDb; 224308-BSU08290; -.
DR EnsemblBacteria; CAB12658; CAB12658; BSU_08290.
DR GeneID; 936171; -.
DR KEGG; bsu:BSU08290; -.
DR PATRIC; fig|224308.179.peg.895; -.
DR eggNOG; COG4585; Bacteria.
DR InParanoid; P94438; -.
DR OrthoDB; 199946at2; -.
DR PhylomeDB; P94438; -.
DR BioCyc; BSUB:BSU08290-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..400
FT /note="Sensor histidine kinase LnrJ"
FT /id="PRO_0000360783"
FT TOPO_DOM 1..2
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 190..385
FT /note="Histidine kinase"
FT /evidence="ECO:0000255"
FT MOD_RES 201
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P13799"
FT MUTAGEN 201
FT /note="H->N: Mutant is sensitive to linearmycins."
FT /evidence="ECO:0000269|PubMed:26647299"
SQ SEQUENCE 400 AA; 44543 MW; 9FA89B7D8149BEAD CRC64;
MKALFFTRMF TLMVSCLMYL SIVKEDNWFG YVFIAAGAAM YAANHVLLTK ETNAIWFCLI
DIAIGFSFGF IFPGTGLFII MLCPVAVAFF LRGFPKRTAW SVLCLSSILF LTVLIRTYAM
FGNEFVIDHL TSMTFVVFCG VVGKLIRKLL DAQDTAKQQF QELTESHLAL SAAHQELHLY
AKQVEELTAI YERNRMAREI HDTVGHKMTA LLVQLQLLRE WQKRDSQKAD ETVGVCETLA
REALDDVRLS VRTLQTENDP SLIESLKQLT EDFCKNAGVT TEFAVSGDPA IIPLSLHPTL
IRTVQEALTN AKRHGGAAAC SIQLACTTDS ISLVIKDDGK GNPEAALGFG LLNMKKRAAE
HGGMIRFESE RDQGFTVNAE FSLANKKWSF GPVQQKESLS
//
