COMQ_BACSU
ID COMQ_BACSU Reviewed; 299 AA.
AC P33690;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Tryptophan prenyltransferase ComQ {ECO:0000305};
DE EC=2.5.1.- {ECO:0000269|PubMed:31670609};
DE AltName: Full=Competence regulatory protein ComQ {ECO:0000305};
GN Name=comQ {ECO:0000303|PubMed:1715859}; OrderedLocusNames=BSU31710;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=1715859; DOI=10.1128/jb.173.18.5685-5693.1991;
RA Weinrauch Y., Msadek T., Kunst F., Dubnau D.;
RT "Sequence and properties of comQ, a new competence regulatory gene of
RT Bacillus subtilis.";
RL J. Bacteriol. 173:5685-5693(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL Microbiology 143:2769-2774(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 34.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP POLYMORPHISM IN COMX; COMQ AND COMP.
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 [6]
RP FUNCTION, AND MUTAGENESIS OF ASP-67 AND ASP-71.
RC STRAIN=168 / JH642;
RX PubMed=11751817; DOI=10.1128/jb.184.2.410-419.2002;
RA Bacon Schneider K., Palmer T.M., Grossman A.D.;
RT "Characterization of comQ and comX, two genes required for production of
RT ComX pheromone in Bacillus subtilis.";
RL J. Bacteriol. 184:410-419(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-63.
RC STRAIN=168;
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:1715859, PubMed:11751817).
CC Involved in the maturation of the competence pheromone ComX
CC (PubMed:11751817, PubMed:31670609). Acts by catalyzing the transfer of
CC a farnesyl group on the ComX pheromone (PubMed:31670609). Shows weak
CC geranylation activity with geranyl diphosphate (GPP) (PubMed:31670609).
CC {ECO:0000269|PubMed:11751817, ECO:0000269|PubMed:1715859,
CC ECO:0000269|PubMed:31670609}.
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:31670609};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68385;
CC Evidence={ECO:0000269|PubMed:31670609};
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 -!- INDUCTION: Expression is maximal early in growth and declines as the
CC cells approach the stationary phase. {ECO:0000269|PubMed:1715859}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene prevents the development
CC of competence as well as the transcription of comG, a late competence
CC operon (PubMed:1715859). Disruption also decreases the expression of
CC srfA, a regulatory operon needed for the expression of competence
CC (PubMed:1715859). {ECO:0000269|PubMed:1715859}.
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. {ECO:0000269|PubMed:11133937}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; M71283; AAA22323.1; -; Genomic_DNA.
DR EMBL; Z93932; CAB07902.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15159.2; -; Genomic_DNA.
DR PIR; A38111; A38111.
DR RefSeq; NP_391049.2; NC_000964.3.
DR RefSeq; WP_003243039.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P33690; -.
DR SMR; P33690; -.
DR STRING; 224308.BSU31710; -.
DR SwissLipids; SLP:000001948; -.
DR PaxDb; P33690; -.
DR EnsemblBacteria; CAB15159; CAB15159; BSU_31710.
DR GeneID; 937180; -.
DR KEGG; bsu:BSU31710; -.
DR PATRIC; fig|224308.179.peg.3436; -.
DR eggNOG; COG0142; Bacteria.
DR OMA; QIANDHH; -.
DR BioCyc; BSUB:BSU31710-MON; -.
DR Proteomes; UP000001570; 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; IBA:GO_Central.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="Tryptophan prenyltransferase ComQ"
FT /id="PRO_0000090014"
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 63
FT /note="S->F: Reduces the farnesylation activity using FPP
FT as the prenyl donor, but geranylation activity using GPP is
FT comparable to that of the wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:31670609"
FT MUTAGEN 67
FT /note="D->E: Loss of activity. Cannot complement the null
FT mutant."
FT /evidence="ECO:0000269|PubMed:11751817"
FT MUTAGEN 71
FT /note="D->E: Loss of activity. Cannot complement the null
FT mutant."
FT /evidence="ECO:0000269|PubMed:11751817"
FT CONFLICT 34
FT /note="T -> S (in Ref. 1; AAA22323 and 2; CAB07902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34218 MW; FC8300C47D8790F8 CRC64;
MKEIVEQNIF NEDLSQLLYS FIDSKETFSF AESTILHYVV FGGENLDVAT RLGAGIEILI
LSSDIMDDLE DEDNHHALWM KINRSESLNA ALSLYTVGLT SIYSLNNNPL IFKYVLKYVN
EAMQGQHDDI TNKSKTEDES LEVIRLKCGS LIALANVAGV LLATGEYNET VERYSYYKGI
IAQISGDYYV LLSGNRSDIE KNKHTLIYLY LKRLFNDASE DLLYLISHKD LYYKSLLDKE
KFQEKLIKAG VTQYISVLLE IYKQKCISAI EQLNLDKEKK ELIKECLLSY TKGDTRCKT
