PQSC_PSEAE
ID PQSC_PSEAE Reviewed; 348 AA.
AC Q9I4X1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=2-heptyl-4(1H)-quinolone synthase subunit PqsC {ECO:0000305};
DE EC=2.3.1.230 {ECO:0000269|PubMed:24239007, ECO:0000269|PubMed:26811339};
GN Name=pqsC {ECO:0000303|PubMed:24239007};
GN OrderedLocusNames=PA0998 {ECO:0000312|EMBL:AAG04387.1};
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, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, ACTIVE SITE, MUTAGENESIS OF CYS-129, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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) OF 2-348 IN COMPLEX WITH PQSB,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF HIS-269 AND VAL-299.
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. First, PqsC acquires an octanoyl group from octanoyl-CoA and
CC forms an octanoyl-PqsC intermediate. Then, together with PqsB, it
CC catalyzes the coupling of 2-ABA with the octanoate group, leading to
CC decarboxylation and dehydration, and resulting in closure of the
CC quinoline ring. {ECO:0000269|PubMed:24239007,
CC ECO:0000269|PubMed:26811339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2-aminobenzoyl)acetate + H(+) + octanoyl-CoA = 2-heptyl-
CC 4(1H)-quinolone + CO2 + CoA + H2O; Xref=Rhea:RHEA:50396,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:62219,
CC ChEBI:CHEBI:131446; EC=2.3.1.230;
CC Evidence={ECO:0000269|PubMed:24239007, ECO:0000269|PubMed:26811339};
CC -!- ACTIVITY REGULATION: Folding of PqsC and binding of octanoate are
CC promoted by PqsB (PubMed:24239007). Binding of the octanoyl group
CC probably increases the binding affinity of the complex for 2-ABA
CC (PubMed:26811339). Activity of the complex is inhibited by 2-
CC aminoacetophenone (2-AA) (PubMed:26811339).
CC {ECO:0000269|PubMed:24239007, ECO:0000269|PubMed:26811339}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.0 uM for octanoyl-CoA (in the presence of PqsB)
CC {ECO:0000269|PubMed:26811339};
CC KM=105 uM for 2-ABA (in the presence of PqsB)
CC {ECO:0000269|PubMed:26811339};
CC Note=kcat is 6.8 sec(-1). {ECO:0000269|PubMed:26811339};
CC -!- SUBUNIT: Forms a tight complex with PqsB. {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; AAG04387.1; -; Genomic_DNA.
DR PIR; A83522; A83522.
DR RefSeq; NP_249689.1; NC_002516.2.
DR RefSeq; WP_003108612.1; NZ_QZGE01000006.1.
DR PDB; 5DWZ; X-ray; 2.04 A; C/D/F/H=2-348.
DR PDB; 6ESZ; X-ray; 1.84 A; A/C=1-348.
DR PDB; 6ET0; X-ray; 1.53 A; A/C=1-348.
DR PDB; 6ET1; X-ray; 2.65 A; A/C/E/G=1-348.
DR PDB; 6ET2; X-ray; 2.60 A; A/C/E/G/I/K/M/O=1-348.
DR PDB; 6ET3; X-ray; 2.25 A; A/C=1-348.
DR PDBsum; 5DWZ; -.
DR PDBsum; 6ESZ; -.
DR PDBsum; 6ET0; -.
DR PDBsum; 6ET1; -.
DR PDBsum; 6ET2; -.
DR PDBsum; 6ET3; -.
DR AlphaFoldDB; Q9I4X1; -.
DR SMR; Q9I4X1; -.
DR STRING; 287.DR97_949; -.
DR PaxDb; Q9I4X1; -.
DR PRIDE; Q9I4X1; -.
DR DNASU; 880660; -.
DR EnsemblBacteria; AAG04387; AAG04387; PA0998.
DR GeneID; 880660; -.
DR KEGG; pae:PA0998; -.
DR PATRIC; fig|208964.12.peg.1030; -.
DR PseudoCAP; PA0998; -.
DR HOGENOM; CLU_039592_1_0_6; -.
DR InParanoid; Q9I4X1; -.
DR OMA; MDSNANC; -.
DR PhylomeDB; Q9I4X1; -.
DR BioCyc; MetaCyc:MON-19873; -.
DR BioCyc; PAER208964:G1FZ6-1017-MON; -.
DR BRENDA; 2.3.1.230; 5087.
DR BRENDA; 2.3.1.B38; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..348
FT /note="2-heptyl-4(1H)-quinolone synthase subunit PqsC"
FT /id="PRO_0000441875"
FT ACT_SITE 129
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:24239007,
FT ECO:0000305|PubMed:26811339"
FT ACT_SITE 269
FT /evidence="ECO:0000305|PubMed:26811339"
FT MUTAGEN 129
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24239007"
FT MUTAGEN 269
FT /note="H->A: Alters binding properties for both 2-ABA and
FT 2-AA. Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:26811339"
FT MUTAGEN 299
FT /note="V->N: Has significant activity toward the desamino
FT substrate analog benzoylacetate."
FT /evidence="ECO:0000269|PubMed:26811339"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6ET0"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 186..199
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6ET3"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:6ET3"
FT HELIX 240..256
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6ET0"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:6ET0"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:6ET0"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:6ET0"
SQ SEQUENCE 348 AA; 38239 MW; DBBBDA8DE2B4A559 CRC64;
MHKVKLAAIT CELPARSYEN DDPVFAAVPD LSESWWQFWG VNRRGYFDPR NGENEFSLVV
RAAERLLRSS DTAPDSVDML ICSASSPIMT DAGDVLPDLR GRLYPRMANV LSKQLGLSRA
LPLDSQMECA SFLLNLRLAA SMIRQGKAEK VLVVCSEYIS NLLDFTSRTS TLFADGCAVA
LLTRGDDDSC DLLASAEHSD ATFYEVATGR WRLPENPTGE AKPRLYFSLF SDGQNKMASF
VPTNVPIAMR RALEKAGLGS DDIDYFVFHQ PAPFLVKAWA EGIGARPEQY QLTMGDTGVM
ISVSIPYTLM TGLREGKIRP GDRIVMAGAA TGWGFAAQVW QLGEVLVC
