ID   PME_RALSO               Reviewed;         396 AA.
AC   P58601;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Pectinesterase;
DE            Short=PE;
DE            EC=3.1.1.11;
DE   AltName: Full=Pectin methylesterase;
DE   Flags: Precursor;
GN   Name=pme; OrderedLocusNames=RSp0138; ORFNames=RS02982;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC         [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC         Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC         ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD17289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL646053; CAD17289.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043876793.1; NC_003296.1.
DR   AlphaFoldDB; P58601; -.
DR   SMR; P58601; -.
DR   STRING; 267608.RSp0138; -.
DR   EnsemblBacteria; CAD17289; CAD17289; RSp0138.
DR   GeneID; 60503076; -.
DR   KEGG; rso:RSp0138; -.
DR   PATRIC; fig|267608.8.peg.3608; -.
DR   eggNOG; COG4677; Bacteria.
DR   HOGENOM; CLU_012243_5_0_4; -.
DR   OMA; FNRMWEY; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR033131; Pectinesterase_Asp_AS.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase; Cell wall biogenesis/degradation; Hydrolase; Plasmid;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..396
FT                   /note="Pectinesterase"
FT                   /id="PRO_0000023500"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            231
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   396 AA;  40961 MW;  2CAAD93DFE8D5D60 CRC64;
     MQSKTLYLKA TALLGGCTVF AATALAVTST ATRPQLSSAD ARTYTIAKYL ASFGTIGSLT
     TDNWDPTGGV GAVSGFRANY AVAADGTAQY KTVQAAIDAA VNAGGVARRY ISVKAGIYNE
     LVCVPESAPP ITLYGLDANA GNTQIVYNNA NPTPASGAKT NPCMGTSSNA TVGTLRSATA
     MVRASDFHAR NLTFKNSYVE GTYADNNQSA VALAVRGDKA ILENVSVIGN QDTLFVGATS
     TTTVIRAYFK NSFIQGDTDF IFGAGTAVFH GCTIQYTAAR LGAKAASYIF APSTAPGNPY
     GFLAINSTFN ATGNPPNNSL HLGRAWDQSV SGTSAYINGS SPNGQVVIRD SSLGALIRLA
     DPWGPSTAGR PYCSANCAYS ANRFFEYNNT GAGSGN