Sensor histidine kinase comP - Bacillus subtilis

Names and origin

Protein names

Recommended name:
Sensor histidine kinase comP
EC=2.7.13.3

Gene names

Name:	comP
Ordered Locus Names:	BSU31690

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length	769 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	Sensor in the two-component regulatory system comP/comA involved in a major quorum response pathway that regulates the development of genetic competence. Plays a role in sporulation, at least partly interchangeable with that of spoIIJ. Probably activates comA by phosphorylation. Ref.6
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Autophosphorylates on a histidine and transfers the phosphate group onto an aspartate in comA, thus activating it.
Miscellaneous	The DNA sequences encoding comQ, comX and the N-terminal two-thirds of comP show a striking polymorphism, which determines the specificity of the quorum-sensing system in the different pherotypes of Bacillus.
Sequence similarities	Contains 1 histidine kinase domain.

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Ontologies

Keywords
Biological process	Competence Sporulation Two-component regulatory system
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	establishment of competence for transformation Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: UniProtKB-KW
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 protein dimerization activity Inferred from electronic annotation. Source: InterPro two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 769

769

Sensor histidine kinase comP

PRO_0000074736

Regions

Topological domain

1 – 9

9

Cytoplasmic Potential

Transmembrane

10 – 33

24

Potential

Topological domain

34 – 113

80

Extracellular Potential

Transmembrane

114 – 134

21

Potential

Topological domain

135 – 144

10

Cytoplasmic Potential

Transmembrane

145 – 167

23

Potential

Topological domain

168 – 235

68

Extracellular Potential

Transmembrane

236 – 257

22

Potential

Topological domain

258 – 272

15

Cytoplasmic Potential

Transmembrane

273 – 295

23

Potential

Topological domain

296 – 299

4

Extracellular Potential

Transmembrane

300 – 323

24

Potential

Topological domain

324 – 337

14

Cytoplasmic Potential

Transmembrane

338 – 357

20

Potential

Topological domain

358 – 361

4

Extracellular Potential

Transmembrane

362 – 383

22

Potential

Topological domain

384 – 769

386

Cytoplasmic Potential

Domain

571 – 769

199

Histidine kinase

Amino acid modifications

Modified residue

576

1

Phosphohistidine; by autocatalysis By similarity

Experimental info

Sequence conflict

604

1

S → C in CAA37957. Ref.1

Sequence conflict

604

1

S → C in AAA22319. Ref.1

Sequence conflict

610

1

D → Y in CAA37957. Ref.1

Sequence conflict

610

1

D → Y in AAA22319. Ref.1

Sequence conflict

628

1

E → G in CAA37957. Ref.1

Sequence conflict

628

1

E → G in AAA22319. Ref.1

Sequence conflict

636 – 637

2

QL → PV in CAA37957. Ref.1

Sequence conflict

636 – 637

2

QL → PV in AAA22319. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q99027-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: E5CEACCE278DE5B4
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FASTA

769

89,317

        10         20         30         40         50         60 
MKNLIKKFTI AVIVLSILYI SYTTYISMNG IIIGTKIHKN DKSQFMIEEI SESSYGQFVG 

        70         80         90        100        110        120 
LRQADIILKI NKEKPSDKHL KWGYLSHINS LDILRSGKKI HLKDFDLVTL NRPYSFFLFV 

       130        140        150        160        170        180 
LPLFFYFLSI ICIFYILKVN KKRRSFAAYI LILLLLDISI AYISAGGPFR GHIINRYINL 

       190        200        210        220        230        240 
FTFISSPILY LQFIQRYLGE IGKTFLNRIS FLYIIPIFNL GIEFFQDYLQ VDIDFLATLN 

       250        260        270        280        290        300 
LVSFATLTLF SFSAIYLHLN KYKYAEHSFI LKLLILTNTL SFAPFLIFFV LPIIFTGNYI 

       310        320        330        340        350        360 
FPALASASLL VLIPFGLVYQ FVANKMFDIE FILGRMRYYA LLAMIPTLLI VGALVLFDVM 

       370        380        390        400        410        420 
DIQMNPVRQT VFFFVVMFAV FYFKEVMDFK FRLKRFSEKF NYQDSIFKYT QLMRGVTSLQ 

       430        440        450        460        470        480 
QVFKELKNTI LDVLLVSKAY TFEVTPDHKV IFLDKHEVGP DWNFYQEEFE NVTSEIGKII 

       490        500        510        520        530        540 
EVNQGFLMKV GERGGSSYVL LCLSNINTPR LTRDEISWLK TLSFYTSVSM ENVLHIEELM 

       550        560        570        580        590        600 
EHLKDLKQEG TNPIWLKKLM FAIEEKQRSG LARDLHDSVL QDLISLKRQC ELFLGDFKKD 

       610        620        630        640        650        660 
DNPSREEVQD KLVQMNEQMS DVISMTRETC HELRPQLLYD LGLVKALSKL VAHEQERVPF 

       670        680        690        700        710        720 
HIRLNTGRFT ASLDLDSQLN LYRIIQEFLS NAVKHSQATD VLIMLISIQN KIVLHYEDDG 

       730        740        750        760 
VGFDQEKNTE HSMSMGLSGI KERVRALDGR LRIETSEGKG FKADIEIEL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A Bacillus subtilis regulatory gene product for genetic competence and sporulation resembles sensor protein members of the bacterial two-component signal-transduction systems." Weinrauch Y., Penchev R., Dubnau E., Smith I., Dubnau D. Genes Dev. 4:860-872(1990) [PubMed: 2116363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BD630.
[2]	"Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai)." Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H., Duesterhoeft A., Pohl T.M., Weitzenegger T. Microbiology 143:2769-2774(1997) [PubMed: 9274030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"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. Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Sequence and properties of comQ, a new competence regulatory gene of Bacillus subtilis." Weinrauch Y., Msadek T., Kunst F., Dubnau D. J. Bacteriol. 173:5685-5693(1991) [PubMed: 1715859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. Strain: 168.
[5]	"Specificity and genetic polymorphism of the Bacillus competence quorum-sensing system." Tortosa P., Logsdon L., Kraigher B., Itoh Y., Mandic-Mulec I., Dubnau D. J. Bacteriol. 183:451-460(2001) [PubMed: 11133937] [Abstract] Cited for: POLYMORPHISM IN COMX; COMQ AND COMP.
[6]	"Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis." Comella N., Grossman A.D. Mol. Microbiol. 57:1159-1174(2005) [PubMed: 16091051] [Abstract] Cited for: FUNCTION.

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Cross-references

Sequence databases
	X54010 mRNA. Translation: CAA37957.1. Z93932 Genomic DNA. Translation: CAB07903.1. Z99120 Genomic DNA. Translation: CAB15157.1. M22856 Genomic DNA. Translation: AAA22319.1. M71283 Genomic DNA. Translation: AAA22324.1.
PIR	A35848. B69604.
RefSeq	NP_391047.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	938866.
GenomeReviews	Gene locus BSU31690 in contig AL009126_GR.
KEGG	bsu:BSU31690.
NMPDR	fig\|224308.1.peg.3172.
Organism-specific databases
SubtiList	BG10380. comP. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	Q99027.
OMA	Q99027. DGVLQDQ.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3164-MON.
BRENDA	2.7.13.3. 150.
Family and domain databases
InterPro	IPR003594. ATP_bd_ATPase. IPR011712. Sig_transdc_His_kin_sub3_dim/P. IPR005467. Sig_transdc_His_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
Pfam	PF02518. HATPase_c. 1 hit. PF07730. HisKA_3. 1 hit. [Graphical view]
SMART	SM00387. HATPase_c. 1 hit. [Graphical view]
PROSITE	PS50109. HIS_KIN. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

COMP_BACSU

Accession

Primary (citable) accession number: Q99027
Secondary accession number(s): O05226

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 30, 2000
Last modified:	June 16, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents