COMQ_BACNB
ID COMQ_BACNB Reviewed; 315 AA.
AC D4G0R4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Tryptophan prenyltransferase ComQ {ECO:0000305};
DE EC=2.5.1.- {ECO:0000269|PubMed:29665236};
DE AltName: Full=ComX-tryptophan prenyltransferase {ECO:0000303|PubMed:29665236};
GN Name=comQ {ECO:0000303|PubMed:29665236};
GN ORFNames=BSNT_09634 {ECO:0000312|EMBL:BAI86695.2};
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.
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, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
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:29665236).
CC Involved in the maturation of the competence pheromone ComX
CC (PubMed:25855042, PubMed:29665236). Acts by catalyzing the transfer of
CC a farnesyl group on the ComX pheromone (PubMed:25855042,
CC PubMed:29665236). In vitro, can also catalyze the farnesylation of
CC single tryptophan and tryptophan derivatives (PubMed:29665236).
CC {ECO:0000269|PubMed:25855042, ECO:0000269|PubMed:29665236}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + L-tryptophyl-[protein] =
CC (2S,3R)-3-farnesyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:68384, Rhea:RHEA-COMP:15365,
CC Rhea:RHEA-COMP:17488, ChEBI:CHEBI:29954, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763, ChEBI:CHEBI:177368;
CC Evidence={ECO:0000269|PubMed:29665236};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68385;
CC Evidence={ECO:0000269|PubMed:29665236};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29665236};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.348 mM for [53-73]ComX {ECO:0000269|PubMed:29665236};
CC KM=0.691 mM for Fmoc-Trp-OH {ECO:0000269|PubMed:29665236};
CC Note=kcat is 0.18 sec(-1) with [53-73]ComX as substrate.
CC {ECO:0000269|PubMed:29665236};
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; AP011541; BAI86695.2; -; Genomic_DNA.
DR STRING; 86029.AWV81_16295; -.
DR EnsemblBacteria; BAI86695; BAI86695; BSNT_09634.
DR KEGG; bso:BSNT_09634; -.
DR HOGENOM; CLU_079583_0_0_9; -.
DR Proteomes; UP000006805; Chromosome.
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..315
FT /note="Tryptophan prenyltransferase ComQ"
FT /id="PRO_0000454301"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
SQ SEQUENCE 315 AA; 36132 MW; 980EF5FC3277874C CRC64;
MSHLVKWNGR GEVVIEQICL DSVRIKEKMK EIVDENILNE DLKVKLISFI KEKKQFSFAE
LAYYHYIAFD GKNDKAIELL ASGIELLILS ADIFDDIEDK DNLQASWMKL DPSIATNAAT
ALYTLSLQVI GSVSNHPKLL SLTLQYSLQS LQGQHVDLNL TASSESEYIE MIKLKSGSLV
TLPSILGVYL ATGEYNETVE EYSRYLGIVE QIANDHYGLY YPNYNDFKTR HTLAFNYLKN
KFNQSSIDLL NFYAQENHMI NNLEDLKGKL RESGVIQYLN VIKNLAVENF KESFKKLRLD
EQRKNKLLIQ LLRGI
