ID   PLYE_DICD3              Reviewed;         404 AA.
AC   P0C1A5; E0SAZ2; P18210;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Pectate lyase E;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelE; OrderedLocusNames=Dda3937_03371;
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].
RC   STRAIN=3937;
RX   PubMed=2695393; DOI=10.1016/0378-1119(89)90472-1;
RA   Reverchon S., Huang Y., Bourson C., Robert-Baudouy J.;
RT   "Nucleotide sequences of the Erwinia chrysanthemi ogl and pelE genes
RT   negatively regulated by the kdgR gene product.";
RL   Gene 85:125-134(1989).
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: Involved in maceration and soft-rotting of plant tissue.
CC       Pectate lyases have been implicated as pathogenicity factors which
CC       induce maceration or rotting of plant tissue. PelE is sufficient to
CC       induce these effects under laboratory conditions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC         oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC         their non-reducing ends.; EC=4.2.2.2;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLBC
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M33584; AAA24854.1; -; Genomic_DNA.
DR   EMBL; CP002038; ADM99551.1; -; Genomic_DNA.
DR   PIR; JQ0190; WZWCPE.
DR   RefSeq; WP_013318982.1; NC_014500.1.
DR   AlphaFoldDB; P0C1A5; -.
DR   SMR; P0C1A5; -.
DR   STRING; 198628.Dda3937_03371; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   EnsemblBacteria; ADM99551; ADM99551; Dda3937_03371.
DR   GeneID; 9734802; -.
DR   KEGG; ddd:Dda3937_03371; -.
DR   PATRIC; fig|198628.6.peg.3309; -.
DR   eggNOG; COG3866; Bacteria.
DR   HOGENOM; CLU_021894_3_0_6; -.
DR   OMA; GNWNSQY; -.
DR   OrthoDB; 163648at2; -.
DR   BioCyc; DDAD198628:DDA3937_RS15615-MON; -.
DR   BioCyc; MetaCyc:MON-15660; -.
DR   UniPathway; UPA00545; UER00824.
DR   PHI-base; PHI:6855; -.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Calcium; Lyase; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000250"
FT   CHAIN           42..404
FT                   /note="Pectate lyase E"
FT                   /id="PRO_0000233031"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000255"
FT   BINDING         182
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        114
FT                   /note="S -> D (in Ref. 1; AAA24854)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   404 AA;  43066 MW;  59DB45FD21FAA8E4 CRC64;
     MNNSRMSSVS TQKTTGRSAL GTKSALAAII ATTMMVSVAS AASLQTTKAT EAASTGWATQ
     SGGTTGGAKA SSSKIYAVKS ISEFKAALNG TDSSPKIIQV TGAIDISGGK AYTSFDDQKA
     RSQISIPSNT TIIGIGNKGK FTNGSLVVKG VSNVILRNLY IETPVDVAPH YEEGDGWNAE
     WDAVVIDSTD HVWVDHVTIS DGSLTDDKYT TKNGEKYVQH DGSLDIKRGS DYVTVSNSRF
     ELHDKTILIG HSDNNGSQDA GKLRVTFHNN LFDRVGERTP RVRFGSVHAY NNVYVGDVNH
     KAYRYQYSFG IGTSGSLLSE SNAFTIDNMK KISGRDKECS VVKAFNGKIF SDKGSIINGA
     SYNLNGCGFG FSAYSAKIPY KYSAQTITTS LANSISSNAG YGKL