ID   COMQ_BACIU              Reviewed;         279 AA.
AC   P0DV08; Q8VLM0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Tryptophan prenyltransferase ComQ {ECO:0000305};
DE            EC=2.5.1.- {ECO:0000250|UniProtKB:D4G0R4};
DE   AltName: Full=Pre-ComX modifying enzyme {ECO:0000305};
GN   Name=comQ {ECO:0000303|PubMed:12067344};
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / RO-PP-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).
CC   -!- FUNCTION: Part of a major quorum-sensing system that regulates the
CC       development of genetic competence (By similarity). Involved in the
CC       maturation of the competence pheromone ComX (By similarity). Acts by
CC       catalyzing the transfer of a prenyl group on the ComX pheromone (By
CC       similarity). {ECO:0000250|UniProtKB:D4G0R4}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:D4G0R4};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0DV09}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AF456131; AAL67718.1; -; Genomic_DNA.
DR   SMR; P0DV08; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR033965; ComQ.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDG01211; Competence_Regulatory_Protein; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Competence; Magnesium; Membrane; Metal-binding;
KW   Prenyltransferase; Transferase.
FT   CHAIN           1..279
FT                   /note="Tryptophan prenyltransferase ComQ"
FT                   /id="PRO_0000454303"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
SQ   SEQUENCE   279 AA;  32015 MW;  16F332B5A682066B CRC64;
     MKEIVHEKIQ NLDLKEYLIN FIDEKNHFSF GILSFKHYVA LSGNRSSHIL TLAGGIELLI
     LAFDIFDDLE DEDNIEIKWM KIDPSLALNA ATTLYTLGLE TICSISNSAE FHRLTLKYAL
     NAMQGQHEDL RNSPETEEEC IQMMKQKAGS LTAMSAVLAA MLANGEFNQT IEDYAYKIGI
     IKQLENDYYG LVNDQRSDIR KKRKTLIYLF LNRKFNEASE KILKLINSHT SYHSFISDSS
     KFDELLFEAG LNQYVSMLIK LYEEEITASM NQLNINIKL