WSPC_PSEPK
ID WSPC_PSEPK Reviewed; 424 AA.
AC Q88MS8;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable biofilm formation methyltransferase WspC;
DE EC=2.1.1.-;
GN Name=wspC; Synonyms=cheR1; OrderedLocusNames=PP_1490;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP SUBUNIT, BINDING TO S-ADENOSYL-L-METHIONINE, AND GENE NAME.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=23029255; DOI=10.1371/journal.pone.0045810;
RA Munoz-Martinez F., Garcia-Fontana C., Rico-Jimenez M., Alfonso C.,
RA Krell T.;
RT "Genes encoding Cher-TPR fusion proteins are predominantly found in gene
RT clusters encoding chemosensory pathways with alternative cellular
RT functions.";
RL PLoS ONE 7:E45810-E45810(2012).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=23677992; DOI=10.1074/jbc.m113.472605;
RA Garcia-Fontana C., Reyes-Darias J.A., Munoz-Martinez F., Alfonso C.,
RA Morel B., Ramos J.L., Krell T.;
RT "High specificity in CheR methyltransferase function: CheR2 of Pseudomonas
RT putida is essential for chemotaxis, whereas CheR1 is involved in biofilm
RT formation.";
RL J. Biol. Chem. 288:18987-18999(2013).
CC -!- FUNCTION: Involved in biofilm formation. {ECO:0000269|PubMed:23677992}.
CC -!- SUBUNIT: Monomer. The TPR repeat does not mediate self-association.
CC {ECO:0000269|PubMed:23029255}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a dramatic reduction in biofilm
CC formation. {ECO:0000269|PubMed:23677992}.
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DR EMBL; AE015451; AAN67112.1; -; Genomic_DNA.
DR RefSeq; NP_743648.1; NC_002947.4.
DR RefSeq; WP_010952583.1; NC_002947.4.
DR AlphaFoldDB; Q88MS8; -.
DR SMR; Q88MS8; -.
DR STRING; 160488.PP_1490; -.
DR EnsemblBacteria; AAN67112; AAN67112; PP_1490.
DR KEGG; ppu:PP_1490; -.
DR PATRIC; fig|160488.4.peg.1580; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_4_0_6; -.
DR OMA; ETFFFRY; -.
DR PhylomeDB; Q88MS8; -.
DR BioCyc; PPUT160488:G1G01-1581-MON; -.
DR BRENDA; 2.1.1.80; 5092.
DR Proteomes; UP000000556; 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 SMART; SM00028; TPR; 2.
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 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; TPR repeat;
KW Transferase.
FT CHAIN 1..424
FT /note="Probable biofilm formation methyltransferase WspC"
FT /id="PRO_0000424792"
FT DOMAIN 1..263
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT REPEAT 355..388
FT /note="TPR"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 206..207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 46889 MW; DA5B218DDCFDA07A CRC64;
MNEQRFFRFL RERIGLDVES VGAPMVERAL RQRCVAAGAM DLDDYWLRLQ QSADEQQALI
EAVIVPETWF FRYPESFTAL ASLAHKRLAQ LAGARPLRLL SLPCSTGEEP YSLAMALFDA
GMAPGAFLVD GMDISPSSVA KAGQAVYGRN AFRGSELGFR ERYFDALDEG HRLHERVRQQ
VSLRVGNVLD PALASRDGLY DFVFCRNLLI YFDVPTQQRV FEVLKRLLHP QGVLFIGPAE
GSLLARMGMR PLGIAQSFAY VRHEGDSAPL AAAPAQTAKR AFTTLPAPVY PQPSVPLPRS
RRVLPVAARP ARAREHSHEG ASELLAGIAR LANAGASEQA RSECQRYLSQ YPPSAQVYYW
LGLLSDTEGD AQQALSHYRK ALYLEPQHPE ALVHLAALLA AQGDLAGARR LQERAARAGR
ESER
