ID   PLYB_DICCH              Reviewed;         375 AA.
AC   P04959;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Pectate lyase B;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelB;
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=EC16;
RX   PubMed=3536853; DOI=10.1128/jb.168.2.595-606.1986;
RA   Keen N.T., Tamaki S.;
RT   "Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and
RT   their high-level expression in Escherichia coli.";
RL   J. Bacteriol. 168:595-606(1986).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
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. PLADES
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M14510; AAA24847.1; -; Genomic_DNA.
DR   PIR; B25158; WZWCPB.
DR   RefSeq; WP_039999247.1; NZ_JAFCAF010000023.1.
DR   AlphaFoldDB; P04959; -.
DR   SMR; P04959; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   BRENDA; 4.2.2.2; 2141.
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; Disulfide bond; Lyase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..375
FT                   /note="Pectate lyase B"
FT                   /id="PRO_0000024853"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000255"
FT   BINDING         150
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..176
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..374
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  40234 MW;  F3FE75D507B8F883 CRC64;
     MKSLITPIAA GLLLAFSQYS LAADTGGYTK TDGGDVSGAV KKTASSMQDI VNIIEAAKVD
     ANGKKVKGGA YPLVITYTGN EDSLINAAAA NICGQWSKDA RGVEIKDFTK GLTIIGANGS
     SANFGIWIVN SSDIVVRNMR IGYLPGGAQD GDMFRIDNSP NVWLDHNELF AANHECDGTK
     DGDTTFESAI DIKKGATYVT ISYNYIHGVK KVGLSGFSSS DTAERNITYH HNIYSDVNAR
     LPLQRGGNVH AYNNLYTGIT SSGLNVRQNG KALIENNWFE NAVSPVTSRY DGSNFGTWVL
     KGNNITKPAD FATYNITWTP DTKEYRNADT WTSTGTYPTV PYSYSPVSAQ CVKDKLANYA
     GVGKNLATLA SSACK