ID   COMX3_BACMO             Reviewed;          53 AA.
AC   Q9K5K8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=ComX pheromone {ECO:0000303|PubMed:14679219};
DE   AltName: Full=Competence pheromone {ECO:0000305};
DE   Flags: Precursor;
GN   Name=comX {ECO:0000303|PubMed:11133937};
OS   Bacillus mojavensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=72360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POLYMORPHISM IN COMX; COMQ AND COMP.
RC   STRAIN=RO-H-1;
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   [2]
RP   FUNCTION, ISOPRENYLATION AT TRP-51, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=RO-H-1;
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   [3]
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   [4]
RP   GERANYLATION AT TRP-51, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=RO-H-1;
RX   PubMed=17617699; DOI=10.1271/bbb.70245;
RA   Okada M., Yamaguchi H., Sato I., Tsuji F., Qi J., Dubnau D., Sakagami Y.;
RT   "Acid labile ComX pheromone from Bacillus mojavensis RO-H-1.";
RL   Biosci. Biotechnol. Biochem. 71:1807-1810(2007).
CC   -!- FUNCTION: Part of a major quorum-sensing system that regulates the
CC       development of genetic competence (PubMed:12067344). Acts through the
CC       activation of the two-component regulatory system ComP/ComA composed of
CC       a sensor histidine kinase, ComP, and a response regulator, ComA (By
CC       similarity). {ECO:0000250|UniProtKB:P45453,
CC       ECO:0000269|PubMed:12067344}.
CC   -!- SUBUNIT: Interacts directly with the sensor histidine kinase ComP and
CC       stimulates its activity. {ECO:0000250|UniProtKB:P45453}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P45453}.
CC   -!- PTM: Trp-51 is modified by geranylation, which is essential for
CC       activity (PubMed:12067344, PubMed:17617699). Modified by the tryptophan
CC       prenyltransferase ComQ before export to the extracellular environment
CC       (By similarity). The type of isoprenyl derivative differs among the
CC       different pherotypes and depends on ComX primary sequence
CC       (PubMed:12067344, PubMed:14679219). {ECO:0000250|UniProtKB:P45453,
CC       ECO:0000269|PubMed:12067344, ECO:0000269|PubMed:14679219,
CC       ECO:0000269|PubMed:17617699}.
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; AY003901; AAF82177.1; -; Genomic_DNA.
DR   RefSeq; WP_010331692.1; NZ_JACJGF010000001.1.
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   InterPro; IPR009233; Competence_ComX_Bacillus.
DR   Pfam; PF05952; ComX; 1.
PE   1: Evidence at protein level;
KW   Competence; Lipoprotein; Pheromone; Prenylation; Secreted.
FT   PROPEP          1..46
FT                   /evidence="ECO:0000269|PubMed:17617699,
FT                   ECO:0000305|PubMed:12067344"
FT                   /id="PRO_0000454308"
FT   PEPTIDE         47..53
FT                   /note="ComX pheromone"
FT                   /evidence="ECO:0000269|PubMed:17617699,
FT                   ECO:0000305|PubMed:12067344"
FT                   /id="PRO_0000454309"
FT   LIPID           51
FT                   /note="3'-geranyl-2',N2-cyclotryptophan"
FT                   /evidence="ECO:0000269|PubMed:17617699,
FT                   ECO:0000305|PubMed:12067344"
SQ   SEQUENCE   53 AA;  6149 MW;  6C9E995840DA0665 CRC64;
     MQEMVGYLIK YPNVLREVME GNACLLGVDK DQSECIINGF KGLEIYSMLD WKY