COMX_BACSU
ID COMX_BACSU Reviewed; 55 AA.
AC P45453;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ComX pheromone {ECO:0000303|PubMed:11751817};
DE AltName: Full=Competence pheromone {ECO:0000303|PubMed:8168130};
DE Flags: Precursor;
GN Name=comX {ECO:0000303|PubMed:8168130}; OrderedLocusNames=BSU31700;
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 [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 [3]
RP PROTEIN SEQUENCE OF 46-55, FUNCTION, SUBCELLULAR LOCATION, AND MODIFICATION
RP AT TRP-53.
RC STRAIN=168;
RX PubMed=8168130; DOI=10.1016/0092-8674(94)90313-1;
RA Magnuson R., Solomon J., Grossman A.D.;
RT "Biochemical and genetic characterization of a competence pheromone from B.
RT subtilis.";
RL Cell 77:207-216(1994).
RN [4]
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 [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-47; PRO-48; ILE-49; THR-50; ARG-51;
RP GLN-52; TRP-53; GLY-54 AND ASP-55.
RC STRAIN=168 / JH642;
RX PubMed=11751817; DOI=10.1128/jb.184.2.410-419.2002;
RA Bacon Schneider K., Palmer T.M., Grossman A.D.;
RT "Characterization of comQ and comX, two genes required for production of
RT ComX pheromone in Bacillus subtilis.";
RL J. Bacteriol. 184:410-419(2002).
RN [6]
RP FUNCTION, SUBUNIT, ISOPRENYLATION AT TRP-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=168;
RX PubMed=12067344; DOI=10.1046/j.1365-2958.2002.02977.x;
RA Ansaldi M., Marolt D., Stebe T., Mandic-Mulec I., Dubnau D.;
RT "Specific activation of the Bacillus quorum-sensing systems by
RT isoprenylated pheromone variants.";
RL Mol. Microbiol. 44:1561-1573(2002).
RN [7]
RP POLYMORPHISM, AND DETERMINANTS OF MODIFICATION SPECIFICITY.
RX PubMed=14679219; DOI=10.1128/jb.186.1.15-21.2004;
RA Ansaldi M., Dubnau D.;
RT "Diversifying selection at the Bacillus quorum-sensing locus and
RT determinants of modification specificity during synthesis of the ComX
RT pheromone.";
RL J. Bacteriol. 186:15-21(2004).
RN [8]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=168 / JH642;
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).
RN [9]
RP ISOPRENYLATION AT TRP-53.
RC STRAIN=168;
RX PubMed=18323630; DOI=10.1271/bbb.80006;
RA Okada M., Yamaguchi H., Sato I., Tsuji F., Dubnau D., Sakagami Y.;
RT "Chemical structure of posttranslational modification with a farnesyl group
RT on tryptophan.";
RL Biosci. Biotechnol. Biochem. 72:914-918(2008).
CC -!- FUNCTION: Part of a major quorum-sensing system that regulates the
CC development of genetic competence (PubMed:8168130, PubMed:11751817,
CC PubMed:16091051, PubMed:12067344). Acts through the activation of the
CC two-component regulatory system ComP/ComA composed of a sensor
CC histidine kinase, ComP, and a response regulator, ComA (PubMed:8168130,
CC PubMed:16091051). Activation of ComA leads to the direct regulation of
CC over 20 genes and expression of over 150 additional genes, including
CC those involved in competence development, appears to be controlled
CC indirectly (PubMed:16091051). Under certain conditions plays a role in
CC sporulation (PubMed:8168130). {ECO:0000269|PubMed:11751817,
CC ECO:0000269|PubMed:12067344, ECO:0000269|PubMed:16091051,
CC ECO:0000269|PubMed:8168130}.
CC -!- SUBUNIT: Interacts directly with the sensor histidine kinase ComP and
CC stimulates its activity. {ECO:0000269|PubMed:12067344,
CC ECO:0000269|PubMed:16091051}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8168130}.
CC -!- PTM: Trp-53 is modified by farnesylation, which is essential for
CC activity (PubMed:8168130, PubMed:12067344, PubMed:18323630). Modified
CC by the tryptophan prenyltransferase ComQ before export to the
CC extracellular environment (PubMed:8168130, PubMed:12067344). The type
CC of isoprenyl derivative differs among the different pherotypes and
CC depends on ComX primary sequence (PubMed:12067344, PubMed:14679219).
CC {ECO:0000269|PubMed:12067344, ECO:0000269|PubMed:14679219,
CC ECO:0000269|PubMed:8168130, ECO:0000305|PubMed:12067344,
CC ECO:0000305|PubMed:18323630, ECO:0000305|PubMed:8168130}.
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. In ComX, the sole conserved residue is the modified
CC tryptophan essential for the activity. {ECO:0000269|PubMed:11133937}.
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DR EMBL; M71283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL009126; CAB15158.1; -; Genomic_DNA.
DR PIR; B38111; B38111.
DR RefSeq; NP_391048.1; NC_000964.3.
DR RefSeq; WP_003242801.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P45453; -.
DR STRING; 224308.BSU31700; -.
DR PaxDb; P45453; -.
DR EnsemblBacteria; CAB15158; CAB15158; BSU_31700.
DR GeneID; 938875; -.
DR KEGG; bsu:BSU31700; -.
DR PATRIC; fig|224308.179.peg.3435; -.
DR BioCyc; BSUB:BSU31700-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005186; F:pheromone activity; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Competence; Direct protein sequencing; Lipoprotein; Pheromone; Prenylation;
KW Reference proteome; Secreted; Sporulation.
FT PROPEP 1..45
FT /evidence="ECO:0000269|PubMed:8168130"
FT /id="PRO_0000020977"
FT PEPTIDE 46..55
FT /note="ComX pheromone"
FT /evidence="ECO:0000269|PubMed:8168130"
FT /id="PRO_0000020978"
FT LIPID 53
FT /note="3'-farnesyl-2',N2-cyclotryptophan"
FT /evidence="ECO:0000305|PubMed:12067344,
FT ECO:0000305|PubMed:18323630, ECO:0000305|PubMed:8168130"
FT MUTAGEN 47
FT /note="D->A: Induction of srfA is delayed approximately 1
FT generation."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 48
FT /note="P->A: Induction of srfA is delayed by 2 generations
FT or more."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 49
FT /note="I->A: Induction of srfA is delayed approximately 1
FT generation."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 50
FT /note="T->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 51
FT /note="R->A: Induction of srfA is delayed by 2 generations
FT or more."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 52
FT /note="Q->A: Induction of srfA is delayed approximately 1
FT generation."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 53
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 54
FT /note="G->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 55
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:11751817"
SQ SEQUENCE 55 AA; 6518 MW; 942D7E152D1846B3 CRC64;
MQDLINYFLN YPEALKKLKN KEACLIGFDV QETETIIKAY NDYYLADPIT RQWGD
