PQSB_PSEAE
ID PQSB_PSEAE Reviewed; 283 AA.
AC Q9I4X2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=2-heptyl-4(1H)-quinolone synthase subunit PqsB {ECO:0000305};
GN Name=pqsB {ECO:0000303|PubMed:24239007};
GN OrderedLocusNames=PA0997 {ECO:0000312|EMBL:AAG04386.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PA14;
RX PubMed=24239007; DOI=10.1016/j.chembiol.2013.09.021;
RA Dulcey C.E., Dekimpe V., Fauvelle D.A., Milot S., Groleau M.C., Doucet N.,
RA Rahme L.G., Lepine F., Deziel E.;
RT "The end of an old hypothesis: the Pseudomonas signaling molecules 4-
RT hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids.";
RL Chem. Biol. 20:1481-1491(2013).
RN [3] {ECO:0007744|PDB:5DWZ}
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH PQSC, FUNCTION,
RP ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26811339; DOI=10.1074/jbc.m115.708453;
RA Drees S.L., Li C., Prasetya F., Saleem M., Dreveny I., Williams P.,
RA Hennecke U., Emsley J., Fetzner S.;
RT "PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas
RT aeruginosa quinolone signal: crystal structure, inhibition, and reaction
RT mechanism.";
RL J. Biol. Chem. 291:6610-6624(2016).
CC -!- FUNCTION: Required for the biosynthesis of the quorum-sensing signaling
CC molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-
CC quinolone (Pseudomonas quinolone signal or PQS), which are important
CC for biofilm formation and virulence. The PqsC/PqsB complex catalyzes
CC the condensation of 2-aminobenzoylacetate (2-ABA) and octanoyl-CoA to
CC form HHQ. PqsB, together with PqsC, catalyzes the coupling of 2-ABA
CC with the octanoate group, leading to decarboxylation and dehydration,
CC and resulting in closure of the quinoline ring. PqsB is probably
CC required for the proper folding of PqsC rather than for a direct
CC enzymatic role in the process. {ECO:0000269|PubMed:24239007,
CC ECO:0000269|PubMed:26811339}.
CC -!- ACTIVITY REGULATION: Activity of the complex is inhibited by 2-
CC aminoacetophenone (2-AA). {ECO:0000269|PubMed:26811339}.
CC -!- SUBUNIT: Forms a tight complex with PqsC. {ECO:0000269|PubMed:24239007,
CC ECO:0000269|PubMed:26811339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24239007}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04386.1; -; Genomic_DNA.
DR PIR; H83521; H83521.
DR RefSeq; NP_249688.1; NC_002516.2.
DR RefSeq; WP_003108611.1; NZ_QZGE01000006.1.
DR PDB; 5DWZ; X-ray; 2.04 A; A/B/E/G=1-283.
DR PDB; 6ESZ; X-ray; 1.84 A; B/D=1-283.
DR PDB; 6ET0; X-ray; 1.53 A; B/D=1-283.
DR PDB; 6ET1; X-ray; 2.65 A; B/D/F/H=1-283.
DR PDB; 6ET2; X-ray; 2.60 A; B/D/F/H/J/L/N/P=1-283.
DR PDB; 6ET3; X-ray; 2.25 A; B/D=1-283.
DR PDBsum; 5DWZ; -.
DR PDBsum; 6ESZ; -.
DR PDBsum; 6ET0; -.
DR PDBsum; 6ET1; -.
DR PDBsum; 6ET2; -.
DR PDBsum; 6ET3; -.
DR AlphaFoldDB; Q9I4X2; -.
DR SMR; Q9I4X2; -.
DR STRING; 287.DR97_950; -.
DR PaxDb; Q9I4X2; -.
DR PRIDE; Q9I4X2; -.
DR DNASU; 883098; -.
DR EnsemblBacteria; AAG04386; AAG04386; PA0997.
DR GeneID; 883098; -.
DR KEGG; pae:PA0997; -.
DR PATRIC; fig|208964.12.peg.1029; -.
DR PseudoCAP; PA0997; -.
DR HOGENOM; CLU_983039_0_0_6; -.
DR OMA; AKRAHVF; -.
DR BioCyc; MetaCyc:MON-19872; -.
DR BioCyc; PAER208964:G1FZ6-1016-MON; -.
DR BRENDA; 2.3.1.230; 5087.
DR BRENDA; 2.3.1.B38; 5087.
DR PHI-base; PHI:5586; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR016039; Thiolase-like.
DR SUPFAM; SSF53901; SSF53901; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..283
FT /note="2-heptyl-4(1H)-quinolone synthase subunit PqsB"
FT /id="PRO_0000441874"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6ET0"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:6ET0"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6ET0"
SQ SEQUENCE 283 AA; 30501 MW; AD02221DA7F263E8 CRC64;
MLIQAVGVNL PPSYVCLEGP LGGERPRAQG DEMLMQRLLP AVREALDEAA VKPEEIDLIV
GLALSPDHLI ENRDIMAPKI GHPLQKVLGA NRAHVFDLTD SSLARALYVV DTLASDQGYR
NVLVVRGESS QGLEVDSESG FALADGALAL LCRPTGKAAF RRGALGGDPA QEWLPLSIPL
NTDIRQVGDV KGHLNLPAQP GLPEAVRAGF TRLAGDFPQL NWVREEWFGQ GRPDGRCLGP
FELASQLRAA QRDRLDELLL ISFDPFGMVV EGVTLELAGE AHA
