ID   COMX2_BACMO             Reviewed;          56 AA.
AC   Q9K5K3;
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:18323630};
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-C-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-54, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=RO-C-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   ISOPRENYLATION AT TRP-54.
RC   STRAIN=RO-C-2;
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: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-54 is modified by farnesylation, which is essential for
CC       activity (PubMed:12067344, PubMed:18323630). 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). {ECO:0000250|UniProtKB:P45453,
CC       ECO:0000269|PubMed:12067344, ECO:0000269|PubMed:18323630}.
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; AY003904; AAF82182.1; -; Genomic_DNA.
DR   EMBL; AF456134; AAL67728.1; -; 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..50
FT                   /evidence="ECO:0000269|PubMed:12067344"
FT                   /id="PRO_0000454306"
FT   PEPTIDE         51..56
FT                   /note="ComX pheromone"
FT                   /evidence="ECO:0000269|PubMed:12067344"
FT                   /id="PRO_0000454307"
FT   MOD_RES         54
FT                   /note="Tryptophan derivative"
FT                   /evidence="ECO:0000269|PubMed:12067344,
FT                   ECO:0000269|PubMed:18323630"
FT   LIPID           54
FT                   /note="3'-farnesyl-2',N2-cyclotryptophan"
FT                   /evidence="ECO:0000269|PubMed:18323630,
FT                   ECO:0000305|PubMed:12067344"
SQ   SEQUENCE   56 AA;  6575 MW;  1EB524BCC033DD12 CRC64;
     MMQDLINYFL SYPEVLKKLK NREACLIGFS SNETETIIKA YNDYHLSSPT TREWDG