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Q99027

- COMP_BACSU

UniProt

Q99027 - COMP_BACSU

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Protein

Sensor histidine kinase ComP

Gene

comP

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphorelay sensor kinase activity Source: InterPro

GO - Biological processi

  1. establishment of competence for transformation Source: UniProtKB-KW
  2. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Competence, Sporulation, Two-component regulatory system

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU31690-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sensor histidine kinase ComP (EC:2.7.13.3)
Gene namesi
Name:comP
Ordered Locus Names:BSU31690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU31690. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 769769Sensor histidine kinase ComPPRO_0000074736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei576 – 5761Phosphohistidine; by autocatalysisPROSITE-ProRule annotation

Post-translational modificationi

Autophosphorylates on a histidine and transfers the phosphate group onto an aspartate in ComA, thus activating it.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ99027.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU31690.

Structurei

3D structure databases

ProteinModelPortaliQ99027.
SMRiQ99027. Positions 31-76, 563-769.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Topological domaini34 – 11380ExtracellularSequence AnalysisAdd
BLAST
Topological domaini135 – 14410CytoplasmicSequence Analysis
Topological domaini168 – 23568ExtracellularSequence AnalysisAdd
BLAST
Topological domaini258 – 27215CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini296 – 2994ExtracellularSequence Analysis
Topological domaini324 – 33714CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini358 – 3614ExtracellularSequence Analysis
Topological domaini384 – 769386CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3324HelicalSequence AnalysisAdd
BLAST
Transmembranei114 – 13421HelicalSequence AnalysisAdd
BLAST
Transmembranei145 – 16723HelicalSequence AnalysisAdd
BLAST
Transmembranei236 – 25722HelicalSequence AnalysisAdd
BLAST
Transmembranei273 – 29523HelicalSequence AnalysisAdd
BLAST
Transmembranei300 – 32324HelicalSequence AnalysisAdd
BLAST
Transmembranei338 – 35720HelicalSequence AnalysisAdd
BLAST
Transmembranei362 – 38322HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini571 – 769199Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 histidine kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4585.
HOGENOMiHOG000246978.
KOiK07680.
OrthoDBiEOG6W9X4M.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
InterProiIPR003594. HATPase_C.
IPR011712. Sig_transdc_His_kin_sub3_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamiPF02518. HATPase_c. 1 hit.
PF07730. HisKA_3. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99027-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNLIKKFTI AVIVLSILYI SYTTYISMNG IIIGTKIHKN DKSQFMIEEI
60 70 80 90 100
SESSYGQFVG LRQGDIILKI NKEKPSDKHL KWGYLSHINS LDILRSGKKI
110 120 130 140 150
HLKDFDLVTL NRPYSFFLFV LPLFFYFLSI ICIFYILKVN KKRRSFAAYI
160 170 180 190 200
LILLLLDISI AYISAGGPFR GHIINRYINL FTFISSPILY LQFIQRYLGE
210 220 230 240 250
IGKTFLNRIS FLYIIPIFNL GIEFFQDYLQ VDIDFLATLN LVSFATLTLF
260 270 280 290 300
SFSAIYLHLN KYKYAEHSFI LKLLILTNTL SFAPFLIFFV LPIIFTGNYI
310 320 330 340 350
FPALASASLL VLIPFGLVYQ FVANKMFDIE FILGRMRYYA LLAMIPTLLI
360 370 380 390 400
VGALVLFDVM DIQMNPVRQT VFFFVVMFAV FYFKEVMDFK FRLKRFSEKF
410 420 430 440 450
NYQDSIFKYT QLMRGVTSLQ QVFKELKNTI LDVLLVSKAY TFEVTPDHKV
460 470 480 490 500
IFLDKHEVGP DWNFYQEEFE NVTSEIGKII EVNQGFLMKV GERGGSSYVL
510 520 530 540 550
LCLSNINTPR LTRDEISWLK TLSFYTSVSM ENVLHIEELM EHLKDLKQEG
560 570 580 590 600
TNPIWLKKLM FAIEEKQRSG LARDLHDSVL QDLISLKRQC ELFLGDFKKD
610 620 630 640 650
DNPCREEVQD KLVQMNEQMS DVISMTRETC HELRPQLLYD LGLVKALSKL
660 670 680 690 700
VAQQQERVPF HIRLNTGRFT ASLDLDSQLN LYRIIQEFLS NAVKHSQATD
710 720 730 740 750
VLIMLISIQN KIVLHYEDDG VGFDQEKNTE HSMSMGLSGI KERVRALDGR
760
LRIETSEGKG FKADIEIEL
Length:769
Mass (Da):89,309
Last modified:July 7, 2009 - v3
Checksum:iAF2DF976EED0EF40
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641G → A in CAA37957. (PubMed:2116363)Curated
Sequence conflicti64 – 641G → A in AAA22319. (PubMed:2116363)Curated
Sequence conflicti64 – 641G → A in CAB07903. (PubMed:9274030)Curated
Sequence conflicti604 – 6041C → S in CAB07903. (PubMed:9274030)Curated
Sequence conflicti610 – 6101D → Y in CAA37957. (PubMed:2116363)Curated
Sequence conflicti610 – 6101D → Y in AAA22319. (PubMed:2116363)Curated
Sequence conflicti628 – 6281E → G in CAA37957. (PubMed:2116363)Curated
Sequence conflicti628 – 6281E → G in AAA22319. (PubMed:2116363)Curated
Sequence conflicti636 – 6372QL → PV in CAA37957. (PubMed:2116363)Curated
Sequence conflicti636 – 6372QL → PV in AAA22319. (PubMed:2116363)Curated
Sequence conflicti653 – 6542QQ → HE in CAA37957. (PubMed:2116363)Curated
Sequence conflicti653 – 6542QQ → HE in AAA22319. (PubMed:2116363)Curated
Sequence conflicti653 – 6542QQ → HE in CAB07903. (PubMed:9274030)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54010 mRNA. Translation: CAA37957.1.
M22856 Genomic DNA. Translation: AAA22319.1.
Z93932 Genomic DNA. Translation: CAB07903.1.
AL009126 Genomic DNA. Translation: CAB15157.2.
M71283 Genomic DNA. Translation: AAA22324.1.
PIRiA35848.
B69604.
RefSeqiNP_391047.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15157; CAB15157; BSU31690.
GeneIDi938866.
KEGGibsu:BSU31690.
PATRICi18978308. VBIBacSub10457_3317.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54010 mRNA. Translation: CAA37957.1 .
M22856 Genomic DNA. Translation: AAA22319.1 .
Z93932 Genomic DNA. Translation: CAB07903.1 .
AL009126 Genomic DNA. Translation: CAB15157.2 .
M71283 Genomic DNA. Translation: AAA22324.1 .
PIRi A35848.
B69604.
RefSeqi NP_391047.2. NC_000964.3.

3D structure databases

ProteinModelPortali Q99027.
SMRi Q99027. Positions 31-76, 563-769.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU31690.

Proteomic databases

PaxDbi Q99027.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15157 ; CAB15157 ; BSU31690 .
GeneIDi 938866.
KEGGi bsu:BSU31690.
PATRICi 18978308. VBIBacSub10457_3317.

Organism-specific databases

GenoListi BSU31690. [Micado ]

Phylogenomic databases

eggNOGi COG4585.
HOGENOMi HOG000246978.
KOi K07680.
OrthoDBi EOG6W9X4M.

Enzyme and pathway databases

BioCyci BSUB:BSU31690-MONOMER.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
InterProi IPR003594. HATPase_C.
IPR011712. Sig_transdc_His_kin_sub3_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view ]
Pfami PF02518. HATPase_c. 1 hit.
PF07730. HisKA_3. 1 hit.
[Graphical view ]
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF55874. SSF55874. 1 hit.
PROSITEi PS50109. HIS_KIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 64; 604 AND 654.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    Strain: 168.
  6. "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] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM IN COMX; COMQ AND COMP.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCOMP_BACSU
AccessioniPrimary (citable) accession number: Q99027
Secondary accession number(s): O05226
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 7, 2009
Last modified: October 29, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3