ID   PLYE2_DICCH             Reviewed;         404 AA.
AC   P0C1A4; P18210;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Pectate lyase E;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelE;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B374;
RX   PubMed=2615652; DOI=10.1111/j.1365-2958.1989.tb00124.x;
RA   van Gijsegem F.;
RT   "Relationship between the pel genes of the pelADE cluster in Erwinia
RT   chrysanthemi strain B374.";
RL   Mol. Microbiol. 3:1415-1424(1989).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X17284; CAA35175.1; -; Genomic_DNA.
DR   PIR; JQ0190; WZWCPE.
DR   AlphaFoldDB; P0C1A4; -.
DR   SMR; P0C1A4; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   UniPathway; UPA00545; UER00824.
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; Secreted; Signal.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000250"
FT   CHAIN           42..404
FT                   /note="Pectate lyase E"
FT                   /id="PRO_0000024858"
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"
SQ   SEQUENCE   404 AA;  43043 MW;  B17C8234445D6AEC CRC64;
     MNNSRMSSVS TQKTTGRSAL GTKSALAAII ATTMMVSVAS AASLQTTKAT EAASTGWATQ
     SGGTTGGAKA SSSKIYAVKS ISEFKAALNG TDSSPKIIQV TGAIDISGGK AYTSFDDQKA
     RSQISIPSNT TIIGIGNKGK FTNGSLVVKG VSNVILRNLY IETPVDVAPH YEEGDGWNAE
     WDAVVIDSTD HVWVDHVTIS DGSFTDDKYT TKNGEKYVQH DGSLDIKRGS DYVTVSNSRF
     ELHDKTILIG HSDNNGSQDA GKLRVTFHNN LFDRVGERTP RVRFGSVHAY NNVYVGDVNH
     KAYRYQYSFG IGTSGSLLSE SNAFTIDNMK KISGRDKECS VVKAFNGKIF SDKGSIINGA
     SYNLNGCGFG FSAYSAKIPY KYSAQTITTS LAGSISSNAG YGKL