COMP_BACSU
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 03-AUG-2022, entry version 144.
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; Firmicutes; 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; M22856; 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_CP053102.1.
DR AlphaFoldDB; Q99027; -.
DR SMR; Q99027; -.
DR STRING; 224308.BSU31690; -.
DR PaxDb; Q99027; -.
DR PRIDE; Q99027; -.
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 OMA; CHELRPQ; -.
DR BioCyc; BSUB:BSU31690-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: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 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; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 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
