ID   WSPC_PSEAE              Reviewed;         422 AA.
AC   Q9HXT5;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable biofilm formation methyltransferase WspC;
DE            EC=2.1.1.-;
GN   Name=wspC; OrderedLocusNames=PA3706;
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, AND GENE NAME.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=16186483; DOI=10.1073/pnas.0507170102;
RA   Hickman J.W., Tifrea D.F., Harwood C.S.;
RT   "A chemosensory system that regulates biofilm formation through modulation
RT   of cyclic diguanylate levels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:14422-14427(2005).
CC   -!- FUNCTION: Involved in biofilm formation. {ECO:0000305|PubMed:16186483}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
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DR   EMBL; AE004091; AAG07093.1; -; Genomic_DNA.
DR   PIR; A83184; A83184.
DR   RefSeq; NP_252395.1; NC_002516.2.
DR   RefSeq; WP_003113845.1; NZ_QZGE01000001.1.
DR   AlphaFoldDB; Q9HXT5; -.
DR   SMR; Q9HXT5; -.
DR   STRING; 287.DR97_4171; -.
DR   PaxDb; Q9HXT5; -.
DR   PRIDE; Q9HXT5; -.
DR   EnsemblBacteria; AAG07093; AAG07093; PA3706.
DR   GeneID; 878238; -.
DR   KEGG; pae:PA3706; -.
DR   PATRIC; fig|208964.12.peg.3877; -.
DR   PseudoCAP; PA3706; -.
DR   HOGENOM; CLU_025854_4_0_6; -.
DR   InParanoid; Q9HXT5; -.
DR   OMA; ETFFFRY; -.
DR   PhylomeDB; Q9HXT5; -.
DR   BioCyc; PAER208964:G1FZ6-3776-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF01739; CheR; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS50123; CHER; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine; TPR repeat;
KW   Transferase.
FT   CHAIN           1..422
FT                   /note="Probable biofilm formation methyltransferase WspC"
FT                   /id="PRO_0000424791"
FT   DOMAIN          1..264
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT   REPEAT          354..387
FT                   /note="TPR"
FT   REGION          289..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..187
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         205..206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  46358 MW;  8085283F0B2508E9 CRC64;
     MNDRFERLLK SRIGLDASSV GSAVIERAVR QRMSGLALHD EDEYWMRLNG SPGEVQALIE
     AVVVPETWFF RYPESFTTLA RLAFERLPSL GGGRALRILS LPCSTGEEPY SIVMALLDAG
     LSEYLFEVDA LDVSARVIER ASLGVYGRNS FRGDELGFRD RHFSEVAEGY QLAEQVRRKV
     RFRCGNLLDP GLLAGEAPYD FVFCRNLLIY FDRPTQSEVV EVLKRLLRPD GAMFIGPAEA
     SLLSQHGMQP IGVPLSFVFR RTSEAPRGAR PKAVSDGARP VVAAAVERAS IRPSPPPPAK
     PRQRLSSLVP PASGQPLASP VGEFDEIARL ADAGQHREAR AACERQLAAR GPSATVFYWL
     GLLSDVAGQE QEAQDFYRKA LYLEPQHAEA LAHLAALLAA RGDHAGARRL QQRAARGVNK
     DG