BCES_BACSU
ID BCES_BACSU Reviewed; 334 AA.
AC O35044;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sensor protein BceS;
DE EC=2.7.13.3;
GN Name=bceS; Synonyms=barB, ytsB; OrderedLocusNames=BSU30390;
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;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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.
RC STRAIN=168;
RX PubMed=14612242; DOI=10.1016/s0378-1097(03)00738-9;
RA Bernard R., Joseph P., Guiseppi A., Chippaux M., Denizot F.;
RT "YtsCD and YwoA, two independent systems that confer bacitracin resistance
RT to Bacillus subtilis.";
RL FEMS Microbiol. Lett. 228:93-97(2003).
RN [5]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=12890034; DOI=10.1046/j.1365-2958.2003.03653.x;
RA Ohki R., Giyanto X., Tateno K., Masuyama W., Moriya S., Kobayashi K.,
RA Ogasawara N.;
RT "The BceRS two-component regulatory system induces expression of the
RT bacitracin transporter, BceAB, in Bacillus subtilis.";
RL Mol. Microbiol. 49:1135-1144(2003).
CC -!- FUNCTION: Member of the two-component regulatory system BceS/BceR
CC involved in the regulation of bacitracin resistance. Activates BceR in
CC response to extracellular bacitracin. {ECO:0000269|PubMed:11717295,
CC ECO:0000269|PubMed:12890034, ECO:0000269|PubMed:14612242}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AF008220; AAC00254.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15017.1; -; Genomic_DNA.
DR PIR; H70000; H70000.
DR RefSeq; NP_390917.1; NC_000964.3.
DR RefSeq; WP_004398652.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O35044; -.
DR SMR; O35044; -.
DR STRING; 224308.BSU30390; -.
DR PaxDb; O35044; -.
DR PRIDE; O35044; -.
DR EnsemblBacteria; CAB15017; CAB15017; BSU_30390.
DR GeneID; 936816; -.
DR KEGG; bsu:BSU30390; -.
DR PATRIC; fig|224308.179.peg.3296; -.
DR eggNOG; COG2205; Bacteria.
DR InParanoid; O35044; -.
DR OMA; YEWLRIH; -.
DR PhylomeDB; O35044; -.
DR BioCyc; BSUB:BSU30390-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
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..334
FT /note="Sensor protein BceS"
FT /id="PRO_0000074709"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 121..326
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 124
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 334 AA; 38765 MW; 2BED582B96FCF482 CRC64;
MIKAFLIERR SWIAAFLFQQ ALMLFIAFVD PSISFGNVLY MVYLCILFFI IFLWFRYRKE
TAFYKSLKTW ENNLDVTAIN EPETPFEAMV ERSIAGQTEH LKQTAARHRL ALENEKDELM
AWIHEVKTPL TAMHLIIDRM EEKALKSQLS YEWLRIHLLL DQQLHQKRIS FIENDLSVEF
IQLQPLIFKE IKDLQSWCIQ KGIGFDIQLE AKEVLSDAKW LAFIIRQLLT NAVKYSEASE
IEIKSFQKGE QTQLQVKDCG RGIDPKDVPR IFDKGFTSTT DHHDQASTGM GLYLAKKAAA
PLLIHIDVES EFGAGTVFTL TFPIRNQFEH VISV
