ID   PLY2_PECCA              Reviewed;         374 AA.
AC   P0C1C1; P11431; Q06112; Q47469;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Pectate lyase 2;
DE            EC=4.2.2.2;
DE   AltName: Full=Pectate lyase B;
DE            Short=PLB;
DE   AltName: Full=Pectate lyase II;
DE            Short=PEL II;
DE   Flags: Precursor;
GN   Name=pel2; Synonyms=pelB;
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Er;
RX   PubMed=1369060; DOI=10.1271/bbb.56.1596;
RA   Yoshida A., Matsuo Y., Kamio Y., Izaki K.;
RT   "Molecular cloning and sequencing of the extracellular pectate lyase II
RT   gene from Erwinia carotovora Er.";
RL   Biosci. Biotechnol. Biochem. 56:1596-1600(1992).
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; S51475; AAC60422.1; -; Genomic_DNA.
DR   PIR; JC1313; JC1313.
DR   RefSeq; WP_039492150.1; NZ_CP034938.1.
DR   AlphaFoldDB; P0C1C1; -.
DR   SMR; P0C1C1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   PRIDE; P0C1C1; -.
DR   GeneID; 51391440; -.
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                   /evidence="ECO:0000250"
FT   CHAIN           23..374
FT                   /note="Pectate lyase 2"
FT                   /id="PRO_0000024850"
FT   ACT_SITE        239
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        350..373
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  40380 MW;  FAE3FD00ACD29ED5 CRC64;
     MKYLLPTAAA GLLLLAAQPA MAANTGGYAT TDGGEVSGAV KKTARSMKEI VDIIEAAQVD
     SKGKKVKGGA YPLIITYSGN EDSLIKAAEK NICGQWSKDA RGVQIKEFTK GITIQGTNGS
     SANFGVWIVN SSNVVVRNMR FGYMPGGAQD GDAIRIDNSP NVWIDHNEIF AKNFECKGTP
     DNDTTFESAV DIKKGSTNVT VSYNYIHGIK KVGLSGASNT DTGRNLTYHH NIYRDVNSRL
     PLQRGGLVHA YNNLYDGITG SGFNVRQKGI ALIESNWFEN ALNPVTARND SSNFGTWELR
     NNNITSPSDF AKYKITWGKP SSPHINADNW KSTGKFPSIS YKYTPVSAQC VKDKLANYAG
     VGKNLAVLTA ANCK