O35044 (BCES_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sensor protein BceS
EC=2.7.13.3

Gene names

Name:	bceS
Synonyms:	barB, ytsB
Ordered Locus Names:	BSU30390

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Member of the two-component regulatory system BceS/BceR involved in the regulation of bacitracin resistance. Activates BceR in response to extracellular bacitracin. Ref.3 Ref.4 Ref.5
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subcellular location	Cell membrane; Multi-pass membrane protein Probable.
Sequence similarities	Contains 1 histidine kinase domain.

Ontologies

Keywords
Biological process	Two-component regulatory system
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 334	334	Sensor protein BceS		PRO_0000074709
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 33	21	Helical; Potential
	Topological domain	34	1	Extracellular Potential
	Transmembrane	35 – 55	21	Helical; Potential
	Topological domain	56 – 334	279	Cytoplasmic Potential
	Domain	121 – 326	206	Histidine kinase
Amino acid modifications
	Modified residue	124	1	Phosphohistidine; by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O35044 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 2BED582B96FCF482	FASTA	334	38,765
	10 20 30 40 50 60 MIKAFLIERR SWIAAFLFQQ ALMLFIAFVD PSISFGNVLY MVYLCILFFI IFLWFRYRKE 70 80 90 100 110 120 TAFYKSLKTW ENNLDVTAIN EPETPFEAMV ERSIAGQTEH LKQTAARHRL ALENEKDELM 130 140 150 160 170 180 AWIHEVKTPL TAMHLIIDRM EEKALKSQLS YEWLRIHLLL DQQLHQKRIS FIENDLSVEF 190 200 210 220 230 240 IQLQPLIFKE IKDLQSWCIQ KGIGFDIQLE AKEVLSDAKW LAFIIRQLLT NAVKYSEASE 250 260 270 280 290 300 IEIKSFQKGE QTQLQVKDCG RGIDPKDVPR IFDKGFTSTT DHHDQASTGM GLYLAKKAAA 310 320 330 PLLIHIDVES EFGAGTVFTL TFPIRNQFEH VISV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems." Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T., Fujita Y. J. Bacteriol. 183:7365-7370(2001) [PubMed: 11717295] [Abstract] Cited for: FUNCTION.
[4]	"YtsCD and YwoA, two independent systems that confer bacitracin resistance to Bacillus subtilis." Bernard R., Joseph P., Guiseppi A., Chippaux M., Denizot F. FEMS Microbiol. Lett. 228:93-97(2003) [PubMed: 14612242] [Abstract] Cited for: FUNCTION. Strain: 168.
[5]	"The BceRS two-component regulatory system induces expression of the bacitracin transporter, BceAB, in Bacillus subtilis." Ohki R., Giyanto X., Tateno K., Masuyama W., Moriya S., Kobayashi K., Ogasawara N. Mol. Microbiol. 49:1135-1144(2003) [PubMed: 12890034] [Abstract] Cited for: FUNCTION. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF008220 Genomic DNA. Translation: AAC00254.1. AL009126 Genomic DNA. Translation: CAB15017.1.
PIR	H70000.
RefSeq	NP_390917.1. NC_000964.3.
3D structure databases
ProteinModelPortal	O35044.
SMR	O35044. Positions 178-326.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000001576; EBBACP00000001576; EBBACG00000001574.
GeneID	936816.
GenomeReviews	Gene locus BSU30390 in contig AL009126_GR.
KEGG	bsu:BSU30390.
NMPDR	fig|224308.1.peg.3042.
PATRIC	18977980. VBIBacSub10457_3178.
Organism-specific databases
GenoList	BSU30390. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000032037.
HOGENOM	HBG305212.
OMA	YEWLRIH.
PhylomeDB	O35044.
ProtClustDB	CLSK873747.
Enzyme and pathway databases
BioCyc	BSUB:BSU30390-MONOMER.
Family and domain databases
InterPro	IPR003594. ATPase-like_ATP-bd. IPR004358. Sig_transdc_His_kin-like_C. IPR003661. Sig_transdc_His_kin_sub1_dim/P. IPR005467. Sig_transdc_His_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
KO	K11629.
Pfam	PF02518. HATPase_c. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
SMART	SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit.
PROSITE	PS50109. HIS_KIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BCES_BACSU

Accession

Primary (citable) accession number: O35044

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 2, 2004
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program