COMX_BACNB
ID COMX_BACNB Reviewed; 73 AA.
AC D4G0R3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=ComX pheromone {ECO:0000303|PubMed:25855042};
DE AltName: Full=Competence pheromone {ECO:0000305};
DE Flags: Precursor;
GN Name=comX {ECO:0000303|PubMed:29665236};
GN ORFNames=BSNT_09633 {ECO:0000312|EMBL:BAI86694.1};
OS Bacillus subtilis subsp. natto (strain BEST195).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=645657;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEST195;
RX PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA Itaya M., Sakakibara Y.;
RT "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT from very short read data.";
RL BMC Genomics 11:243-243(2010).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=BEST195;
RX PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT long reads with high-quality short reads.";
RL PLoS ONE 9:E109999-E109999(2014).
RN [3]
RP FUNCTION, ISOPRENYLATION AT TRP-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=25855042; DOI=10.1080/09168451.2015.1032884;
RA Hayashi S., Usami S., Nakamura Y., Ozaki K., Okada M.;
RT "Identification of a quorum sensing pheromone posttranslationally
RT farnesylated at the internal tryptophan residue from Bacillus subtilis
RT subsp. natto.";
RL Biosci. Biotechnol. Biochem. 79:1567-1569(2015).
RN [4]
RP FUNCTION, ISOPRENYLATION AT TRP-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26276536; DOI=10.1016/j.bmcl.2015.07.083;
RA Okada M., Nakamura Y., Hayashi S., Ozaki K., Usami S.;
RT "Chemical structure and biological activity of a quorum sensing pheromone
RT from Bacillus subtilis subsp. natto.";
RL Bioorg. Med. Chem. Lett. 25:4293-4296(2015).
RN [5]
RP FUNCTION, ISOPRENYLATION AT TRP-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29665236; DOI=10.1002/cbic.201800174;
RA Sugita T., Okada M., Nakashima Y., Tian T., Abe I.;
RT "A tryptophan prenyltransferase with broad substrate tolerance from
RT Bacillus subtilis subsp. natto.";
RL ChemBioChem 19:1396-1399(2018).
CC -!- FUNCTION: Part of a major quorum-sensing system that regulates the
CC development of genetic competence (PubMed:25855042, PubMed:26276536,
CC PubMed:29665236). Acts through the activation of the two-component
CC regulatory system ComP/ComA composed of a sensor histidine kinase,
CC ComP, and a response regulator, ComA (By similarity). Activates the
CC expression of the genes for biosynthesis of poly-gamma-glutamic acid
CC (gamma-PGA), which is involved in biofilm formation in B.subtilis natto
CC (PubMed:25855042, PubMed:26276536). {ECO:0000250|UniProtKB:P45453,
CC ECO:0000269|PubMed:25855042, ECO:0000269|PubMed:26276536,
CC ECO:0000269|PubMed:29665236}.
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:25855042, PubMed:26276536, PubMed:29665236). Modified
CC by the tryptophan prenyltransferase ComQ before export to the
CC extracellular environment (PubMed:25855042, PubMed:29665236).
CC {ECO:0000269|PubMed:25855042, ECO:0000269|PubMed:26276536,
CC ECO:0000269|PubMed:29665236}.
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DR EMBL; AP011541; BAI86694.1; -; Genomic_DNA.
DR RefSeq; WP_014480704.1; NC_017196.2.
DR SMR; D4G0R3; -.
DR EnsemblBacteria; BAI86694; BAI86694; BSNT_09633.
DR KEGG; bso:BSNT_09633; -.
DR PATRIC; fig|645657.3.peg.4099; -.
DR HOGENOM; CLU_2696611_0_0_9; -.
DR Proteomes; UP000006805; 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 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..52
FT /evidence="ECO:0000269|PubMed:25855042,
FT ECO:0000269|PubMed:29665236"
FT /id="PRO_0000454310"
FT PEPTIDE 53..58
FT /note="ComX pheromone"
FT /evidence="ECO:0000269|PubMed:25855042,
FT ECO:0000269|PubMed:29665236"
FT /id="PRO_0000454311"
FT PROPEP 59..73
FT /evidence="ECO:0000269|PubMed:25855042,
FT ECO:0000269|PubMed:29665236"
FT /id="PRO_0000454312"
FT LIPID 54
FT /note="3'-farnesyl-2',N2-cyclotryptophan"
FT /evidence="ECO:0000269|PubMed:25855042,
FT ECO:0000269|PubMed:26276536, ECO:0000269|PubMed:29665236"
SQ SEQUENCE 73 AA; 8514 MW; 462293A977D441D8 CRC64;
MKHIDKIISH LVNNPEAFDQ FKNGNLTLLN INEKEKKAIL YAFEQGEVPR TSKWPPIEAI
SNFFEDDKRK SLI
