ID   COMX1_BACMO             Reviewed;          54 AA.
AC   Q9K5K2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 32.
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-B-2;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ISOPRENYLATION AT TRP-51, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=RO-B-2;
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).
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 isoprenylation, probably by geranylation,
CC       which is essential for activity (PubMed:12067344). Modified by the
CC       tryptophan prenyltransferase ComQ before export to the extracellular
CC       environment (By similarity). The type of isoprenyl derivative differs
CC       among the 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   -!- 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; AY003905; AAF82183.1; -; Genomic_DNA.
DR   EMBL; AF456135; AAL67731.1; -; Genomic_DNA.
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:12067344"
FT                   /id="PRO_0000454304"
FT   PEPTIDE         47..54
FT                   /note="ComX pheromone"
FT                   /evidence="ECO:0000269|PubMed:12067344"
FT                   /id="PRO_0000454305"
FT   LIPID           51
FT                   /note="3'-geranyl-2',N2-cyclotryptophan"
FT                   /evidence="ECO:0000305|PubMed:12067344"
SQ   SEQUENCE   54 AA;  6008 MW;  A129DE15462DA5ED CRC64;
     MQEIVGYLVK NPEVLDEVMK GRASLLNIDK DQLKSIVDAF GGLQIYTNGN WVPS