PMEB_DICD3
ID PMEB_DICD3 Reviewed; 433 AA.
AC Q47474; E0SL58;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pectinesterase B;
DE Short=PE B;
DE EC=3.1.1.11 {ECO:0000269|PubMed:8830237};
DE AltName: Full=Pectin methylesterase B;
DE Flags: Precursor;
GN Name=pemB {ECO:0000303|PubMed:8830237}; OrderedLocusNames=Dda3937_03435;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, PROBABLE TOPOLOGY, DIACYLGLYCEROL AT CYS-22, AND
RP PALMITOYLATION AT CYS-22.
RC STRAIN=3937;
RX PubMed=8830237; DOI=10.1046/j.1365-2958.1996.389922.x;
RA Shevchik V.E., Condemine G., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.;
RT "Characterization of pectin methylesterase B, an outer membrane lipoprotein
RT of Erwinia chrysanthemi 3937.";
RL Mol. Microbiol. 19:455-466(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
CC -!- FUNCTION: Probably involved in the degradation of methylated
CC oligogalacturonides present in the periplasm. More active on methylated
CC oligogalacturides than on pectin. {ECO:0000269|PubMed:8830237}.
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 Evidence={ECO:0000269|PubMed:8830237};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:8830237};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:8830237};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:8830237};
CC Lipid-anchor {ECO:0000269|PubMed:8830237}. Note=Probably active in the
CC periplasm. {ECO:0000305|PubMed:8830237}.
CC -!- INDUCTION: By polygalacturonates and galacturonate. Repressed by kdgR.
CC {ECO:0000269|PubMed:8830237}.
CC -!- DISRUPTION PHENOTYPE: Decreased growth on methylated oligogalacturides;
CC double pemA-pemB deletions grow very poorly on methylated
CC oligogalacturides. {ECO:0000269|PubMed:8830237}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
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DR EMBL; X84665; CAA59151.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98093.1; -; Genomic_DNA.
DR PIR; S70914; S70914.
DR RefSeq; WP_013317553.1; NC_014500.1.
DR AlphaFoldDB; Q47474; -.
DR SMR; Q47474; -.
DR STRING; 198628.Dda3937_03435; -.
DR EnsemblBacteria; ADM98093; ADM98093; Dda3937_03435.
DR GeneID; 9733317; -.
DR KEGG; ddd:Dda3937_03435; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_012243_5_0_6; -.
DR OMA; FNRLWEY; -.
DR OrthoDB; 1095798at2; -.
DR BioCyc; DDAD198628:DDA3937_RS08920-MON; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:ASAP.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IDA:ASAP.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045488; P:pectin metabolic process; IDA:ASAP.
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; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 1: Evidence at protein level;
KW Aspartyl esterase; Cell outer membrane; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..21
FT CHAIN 22..433
FT /note="Pectinesterase B"
FT /id="PRO_0000023499"
FT TOPO_DOM 22..433
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:8830237"
FT ACT_SITE 259
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 292
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8830237"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:8830237"
FT CONFLICT 245..258
FT /note="DRVQLENVRLLSRQ -> ESGATGKCPPAQPS (in Ref. 1;
FT CAA59151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 47190 MW; 73C2B9E8ED50281F CRC64;
MSLTHYSGLA AAVSMSLILT ACGGQTPNSA RFQPVFPGTV SRPVLSAQEA GRFTPQHYFA
HGGEYAKPVA DGWTPTPIDT SRVTAAYVVG PRAGVAGATH TSIQQAVNAA LRQHPGQTRV
YIKLLPGTYT GTVYVPEGAP PLTLFGAGDR PEQVVVSLAL DSMMSPADYR ARVNPHGQYQ
PADPAWYMYN ACATKAGATI NTTCSAVMWS QSNDFQLKNL TVVNALLDTV DSGTHQAVAL
RTDGDRVQLE NVRLLSRQDT FFVNTSDRQN SYVTDHYSRA YIKDSYIEGD VDYVFGRATA
VFDRVRFHTV SSRGSKEAYV FAPDSIPSVK YGFLVINSQL TGDNGYRGAQ KAKLGRAWDQ
GAKQTGYLPG KTANGQLVIR DSTIDSSYDL ANPWGAAATT DRPFKGNISP QRDLDDIHFN
RLWEYNTQVL LHE
