RPAI_RHOPA
ID RPAI_RHOPA Reviewed; 218 AA.
AC Q6NCZ6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=4-coumaroyl-homoserine lactone synthase {ECO:0000305};
DE EC=2.3.1.229 {ECO:0000269|PubMed:18563084};
DE AltName: Full=p-coumaryl-homoserine lactone synthase {ECO:0000303|PubMed:18563084};
DE Short=pC-HSL synthase {ECO:0000303|PubMed:18563084};
GN Name=rpaI {ECO:0000303|PubMed:18563084};
GN OrderedLocusNames=RPA0320 {ECO:0000312|EMBL:CAE25764.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=18563084; DOI=10.1038/nature07088;
RA Schaefer A.L., Greenberg E.P., Oliver C.M., Oda Y., Huang J.J.,
RA Bittan-Banin G., Peres C.M., Schmidt S., Juhaszova K., Sufrin J.R.,
RA Harwood C.S.;
RT "A new class of homoserine lactone quorum-sensing signals.";
RL Nature 454:595-599(2008).
CC -!- FUNCTION: Catalyzes the synthesis of 4-coumaroyl-homoserine lactone, a
CC quorum-sensing (QS) autoinducer molecule which binds to RpaR
CC transcriptional regulator to regulate expression of QS-dependent genes.
CC {ECO:0000269|PubMed:18563084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-coumaroyl-CoA + S-adenosyl-L-methionine = CoA + H(+) + N-(4-
CC coumaroyl)-L-homoserine lactone + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:37491, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74974; EC=2.3.1.229;
CC Evidence={ECO:0000269|PubMed:18563084};
CC -!- INDUCTION: Repressed by RpaR in the absence of 4-coumaroyl-homoserine
CC lactone. Induced by 4-coumaroyl-homoserine lactone.
CC {ECO:0000269|PubMed:18563084}.
CC -!- SIMILARITY: Belongs to the autoinducer synthase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00533}.
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DR EMBL; BX572593; CAE25764.1; -; Genomic_DNA.
DR RefSeq; WP_011155888.1; NC_005296.1.
DR PDB; 6WN0; X-ray; 1.85 A; A/B=1-213.
DR PDBsum; 6WN0; -.
DR AlphaFoldDB; Q6NCZ6; -.
DR SMR; Q6NCZ6; -.
DR STRING; 258594.RPA0320; -.
DR PRIDE; Q6NCZ6; -.
DR DNASU; 2691374; -.
DR EnsemblBacteria; CAE25764; CAE25764; RPA0320.
DR GeneID; 66891330; -.
DR KEGG; rpa:RPA0320; -.
DR eggNOG; COG3916; Bacteria.
DR HOGENOM; CLU_085711_3_0_5; -.
DR OMA; EIYVKQR; -.
DR PhylomeDB; Q6NCZ6; -.
DR BioCyc; RPAL258594:TX73_RS01655-MON; -.
DR BRENDA; 2.3.1.229; 5412.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001690; Autoind_synthase.
DR PANTHER; PTHR39322; PTHR39322; 1.
DR Pfam; PF00765; Autoind_synth; 1.
DR PRINTS; PR01549; AUTOINDCRSYN.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51187; AUTOINDUCER_SYNTH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autoinducer synthesis; Quorum sensing; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..218
FT /note="4-coumaroyl-homoserine lactone synthase"
FT /id="PRO_0000430601"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6WN0"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:6WN0"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6WN0"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:6WN0"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:6WN0"
SQ SEQUENCE 218 AA; 24646 MW; 1A3C248A8D1AD765 CRC64;
MQVHVIRREN RALYAGLLEK YFRIRHQIYV VERGWKELDR PDGREIDQFD TEDAVYLLGV
DNDDIVAGMR MVPTTSPTLL SDVFPQLALA GPVRRPDAYE LSRIFVVPRK RGEHGGPRAE
AVIQAAAMEY GLSIGLSAFT IVLETWWLPR LVDQGWKAKP LGLPQDINGF STTAVIVDVD
DDAWVGICNR RSVPGPTLEW RGLEAIRRHS LPEFQVIS
