COMQ_BACSC
ID COMQ_BACSC Reviewed; 279 AA.
AC P0DV09; 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:0000269|PubMed:22197102, ECO:0000269|PubMed:25036949, ECO:0000269|PubMed:31670609};
DE AltName: Full=Pre-ComX modifying enzyme {ECO:0000305};
GN Name=comQ {ECO:0000303|PubMed:12067344};
OS Bacillus spizizenii (Bacillus subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=96241;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RO-E-2 / NRRL B-23055;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DV3-D-2 / NRRL B-23063;
RA Sabotic J., Cepon U., Cadez P., Mandic Mulec I.;
RT "Variability of Bacillus sp. quorum sensing system.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=RO-E-2 / NRRL B-23055;
RX PubMed=22197102; DOI=10.1016/j.febslet.2011.12.012;
RA Tsuji F., Ishihara A., Kurata K., Nakagawa A., Okada M., Kitamura S.,
RA Kanamaru K., Masuda Y., Murakami K., Irie K., Sakagami Y.;
RT "Geranyl modification on the tryptophan residue of ComXRO-E-2 pheromone by
RT a cell-free system.";
RL FEBS Lett. 586:174-179(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-182; 183-GLN-LEU-184;
RP ASN-186; ASP-187; TYR-188; TYR-189 AND GLY-190.
RC STRAIN=RO-E-2 / NRRL B-23055;
RX PubMed=25036949; DOI=10.1080/09168451.2014.891932;
RA Okada M., Ishihara A., Yamasaki R., Tsuji F., Hayashi S., Usami S.,
RA Sakagami Y.;
RT "A region corresponding to second aspartate-rich motif in tryptophan
RT isoprenylating enzyme, ComQ, serves as a substrate-binding site.";
RL Biosci. Biotechnol. Biochem. 78:550-555(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ILE-49; PHE-63; ASP-68;
RP THR-92; PRO-134; THR-152; ASN-186; GLY-190; LYS-202; SER-234 AND GLU-248.
RC STRAIN=RO-E-2 / NRRL B-23055;
RX PubMed=31670609; DOI=10.1080/09168451.2019.1685371;
RA Hirooka K., Shioda S., Okada M.;
RT "Identification of critical residues for the catalytic activity of ComQ, a
RT Bacillus prenylation enzyme for quorum sensing, by using a simple bioassay
RT system.";
RL Biosci. Biotechnol. Biochem. 84:347-357(2020).
CC -!- FUNCTION: Part of a major quorum-sensing system that regulates the
CC development of genetic competence (PubMed:22197102). Involved in the
CC maturation of the competence pheromone ComX (PubMed:22197102,
CC PubMed:25036949). Acts by catalyzing the transfer of a geranyl group on
CC the ComX pheromone (PubMed:22197102, PubMed:25036949, PubMed:31670609).
CC Cannot use farnesyl diphosphate (FPP) (PubMed:31670609).
CC {ECO:0000269|PubMed:22197102, ECO:0000269|PubMed:25036949,
CC ECO:0000269|PubMed:31670609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + L-tryptophyl-[protein] = (2S,3R)-3-
CC geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophyl-[protein] +
CC diphosphate; Xref=Rhea:RHEA:59492, Rhea:RHEA-COMP:15365, Rhea:RHEA-
CC COMP:15366, ChEBI:CHEBI:29954, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:141127; Evidence={ECO:0000269|PubMed:22197102,
CC ECO:0000269|PubMed:25036949, ECO:0000269|PubMed:31670609};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59493;
CC Evidence={ECO:0000269|PubMed:22197102, ECO:0000269|PubMed:25036949,
CC ECO:0000269|PubMed:31670609};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22197102};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:22197102};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:22197102};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22197102}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AF456138; AAL67739.1; -; Genomic_DNA.
DR EMBL; DQ241785; ABB51993.1; -; Genomic_DNA.
DR SMR; P0DV09; -.
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 1: Evidence at protein level;
KW Cell membrane; Competence; Magnesium; Membrane; Metal-binding;
KW Prenyltransferase; Transferase.
FT CHAIN 1..279
FT /note="Tryptophan prenyltransferase ComQ"
FT /id="PRO_0000454302"
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"
FT MUTAGEN 49
FT /note="I->A: No change in ComX production or secretion."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 63
FT /note="F->S: Shows substantial farnesylation activity when
FT FPP is used, while geranylation activity is severely
FT reduced."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 68
FT /note="D->E: Severely impairs prenylation activity."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 92
FT /note="T->L: No change in ComX production or secretion."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 134
FT /note="P->S: No change in ComX production or secretion."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 152
FT /note="T->I: No change in ComX production or secretion."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 182
FT /note="K->F: Retains 37% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 183..184
FT /note="QL->AA: Retains 65% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 186
FT /note="N->A: Retains 20% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 186
FT /note="N->D: Retains 9% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 186
FT /note="N->G: Cannot activate ComX."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 187
FT /note="D->A,E,N: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 188
FT /note="Y->A: Retains 54% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 189
FT /note="Y->A: Retains 47% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 190
FT /note="G->A: Retains 87% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 190
FT /note="G->D: Retains 75% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:25036949"
FT MUTAGEN 190
FT /note="G->V: Cannot activate ComX."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 202
FT /note="K->N: No change in ComX production or secretion."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 234
FT /note="S->K: No change in ComX production or secretion."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 248
FT /note="E->K: No change in ComX production or secretion."
FT /evidence="ECO:0000269|PubMed:31670609"
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
