ID   COMP_BACSU              Reviewed;         769 AA.
AC   Q99027; O05226;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Sensor histidine kinase ComP;
DE            EC=2.7.13.3;
GN   Name=comP; OrderedLocusNames=BSU31690;
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=BD630;
RX   PubMed=2116363; DOI=10.1101/gad.4.5.860;
RA   Weinrauch Y., Penchev R., Dubnau E., Smith I., Dubnau D.;
RT   "A Bacillus subtilis regulatory gene product for genetic competence and
RT   sporulation resembles sensor protein members of the bacterial two-component
RT   signal-transduction systems.";
RL   Genes Dev. 4:860-872(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA   Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA   Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT   "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT   of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL   Microbiology 143:2769-2774(1997).
RN   [3]
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   [4]
RP   SEQUENCE REVISION TO 64; 604 AND 654.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC   STRAIN=168;
RX   PubMed=1715859; DOI=10.1128/jb.173.18.5685-5693.1991;
RA   Weinrauch Y., Msadek T., Kunst F., Dubnau D.;
RT   "Sequence and properties of comQ, a new competence regulatory gene of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 173:5685-5693(1991).
RN   [6]
RP   POLYMORPHISM IN COMX; COMQ AND COMP.
RX   PubMed=11133937; DOI=10.1128/jb.183.2.451-460.2001;
RA   Tortosa P., Logsdon L., Kraigher B., Itoh Y., Mandic-Mulec I., Dubnau D.;
RT   "Specificity and genetic polymorphism of the Bacillus competence quorum-
RT   sensing system.";
RL   J. Bacteriol. 183:451-460(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=16091051; DOI=10.1111/j.1365-2958.2005.04749.x;
RA   Comella N., Grossman A.D.;
RT   "Conservation of genes and processes controlled by the quorum response in
RT   bacteria: characterization of genes controlled by the quorum-sensing
RT   transcription factor ComA in Bacillus subtilis.";
RL   Mol. Microbiol. 57:1159-1174(2005).
CC   -!- FUNCTION: Sensor in the two-component regulatory system ComP/ComA
CC       involved in a major quorum response pathway that regulates the
CC       development of genetic competence. Plays a role in sporulation, at
CC       least partly interchangeable with that of SpoIIJ. Probably activates
CC       ComA by phosphorylation. {ECO:0000269|PubMed:16091051}.
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; Multi-pass membrane protein.
CC   -!- PTM: Autophosphorylates on a histidine and transfers the phosphate
CC       group onto an aspartate in ComA, thus activating it.
CC   -!- MISCELLANEOUS: The DNA sequences encoding comQ, comX and the N-terminal
CC       two-thirds of comP show a striking polymorphism, which determines the
CC       specificity of the quorum-sensing system in the different pherotypes of
CC       Bacillus.
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DR   EMBL; X54010; CAA37957.1; -; mRNA.
DR   EMBL; AH000865; AAA22319.1; -; Genomic_DNA.
DR   EMBL; Z93932; CAB07903.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15157.2; -; Genomic_DNA.
DR   EMBL; M71283; AAA22324.1; -; Genomic_DNA.
DR   PIR; A35848; A35848.
DR   PIR; B69604; B69604.
DR   RefSeq; NP_391047.2; NC_000964.3.
DR   RefSeq; WP_003242894.1; NZ_CP103783.1.
DR   AlphaFoldDB; Q99027; -.
DR   SMR; Q99027; -.
DR   STRING; 224308.BSU31690; -.
DR   PaxDb; 224308-BSU31690; -.
DR   EnsemblBacteria; CAB15157; CAB15157; BSU_31690.
DR   GeneID; 938866; -.
DR   KEGG; bsu:BSU31690; -.
DR   PATRIC; fig|224308.179.peg.3434; -.
DR   eggNOG; COG4585; Bacteria.
DR   InParanoid; Q99027; -.
DR   OrthoDB; 9781904at2; -.
DR   BioCyc; BSUB:BSU31690-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   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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; IPR005467; His_kinase_dom.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF65; SENSOR HISTIDINE KINASE COMP; 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.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Competence; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Sporulation;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..769
FT                   /note="Sensor histidine kinase ComP"
FT                   /id="PRO_0000074736"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..272
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..361
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..769
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          571..769
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         576
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        64
FT                   /note="G -> A (in Ref. 1; CAA37957/AAA22319 and 2;
FT                   CAB07903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604
FT                   /note="C -> S (in Ref. 2; CAB07903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        610
FT                   /note="D -> Y (in Ref. 1; CAA37957/AAA22319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        628
FT                   /note="E -> G (in Ref. 1; CAA37957/AAA22319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        636..637
FT                   /note="QL -> PV (in Ref. 1; CAA37957/AAA22319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        653..654
FT                   /note="QQ -> HE (in Ref. 1; CAA37957/AAA22319 and 2;
FT                   CAB07903)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   769 AA;  89309 MW;  AF2DF976EED0EF40 CRC64;
     MKNLIKKFTI AVIVLSILYI SYTTYISMNG IIIGTKIHKN DKSQFMIEEI SESSYGQFVG
     LRQGDIILKI NKEKPSDKHL KWGYLSHINS LDILRSGKKI HLKDFDLVTL NRPYSFFLFV
     LPLFFYFLSI ICIFYILKVN KKRRSFAAYI LILLLLDISI AYISAGGPFR GHIINRYINL
     FTFISSPILY LQFIQRYLGE IGKTFLNRIS FLYIIPIFNL GIEFFQDYLQ VDIDFLATLN
     LVSFATLTLF SFSAIYLHLN KYKYAEHSFI LKLLILTNTL SFAPFLIFFV LPIIFTGNYI
     FPALASASLL VLIPFGLVYQ FVANKMFDIE FILGRMRYYA LLAMIPTLLI VGALVLFDVM
     DIQMNPVRQT VFFFVVMFAV FYFKEVMDFK FRLKRFSEKF NYQDSIFKYT QLMRGVTSLQ
     QVFKELKNTI LDVLLVSKAY TFEVTPDHKV IFLDKHEVGP DWNFYQEEFE NVTSEIGKII
     EVNQGFLMKV GERGGSSYVL LCLSNINTPR LTRDEISWLK TLSFYTSVSM ENVLHIEELM
     EHLKDLKQEG TNPIWLKKLM FAIEEKQRSG LARDLHDSVL QDLISLKRQC ELFLGDFKKD
     DNPCREEVQD KLVQMNEQMS DVISMTRETC HELRPQLLYD LGLVKALSKL VAQQQERVPF
     HIRLNTGRFT ASLDLDSQLN LYRIIQEFLS NAVKHSQATD VLIMLISIQN KIVLHYEDDG
     VGFDQEKNTE HSMSMGLSGI KERVRALDGR LRIETSEGKG FKADIEIEL
//