ID   PLY_PSEAV               Reviewed;         379 AA.
AC   P72242;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Pectate lyase;
DE            Short=PL;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelP;
OS   Pseudomonas amygdali pv. lachrymans (Pseudomonas syringae pv. lachrymans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas amygdali.
OX   NCBI_TaxID=53707;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=859;
RA   Bauer D.W., Collmer A.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in bacterial invasion of plants.
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.
CC       {ECO:0000305}.
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DR   EMBL; U75414; AAB17879.1; -; Genomic_DNA.
DR   AlphaFoldDB; P72242; -.
DR   SMR; P72242; -.
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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..379
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024862"
FT   REGION          190..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  40264 MW;  22DBF8AB31949C92 CRC64;
     MLKPHGLTPL ALTGGILVSL LSVSLSAHAE IATDVATTGW ATQNGGTKGG SRAAANNIYT
     VKNAAELKAA LAASGGSNGR IIKERGVIDV SDGKPYTKTS DMKQRARLDI PGKTTIVGTS
     SSAEIREGFF YAKENDVIIR NLTIENPWDP EPVWDPEDGS AGNWNSEYDG LTVEGASNVW
     IDHVTFTDGR RTDDQNGTAN GRPKQHHDGA LDVKNGANYV TISYSVFRNH EKNNLIGSSD
     SKTPDDGKLK VTNHNSLFEN ISSRGPRVRV GQVHLYNNHH IGSTTHKVYP CVYAQGVGKG
     SKIFSERNVL DISGISGCSK VAADYGGSVY RDSGSLVNGS VISCSWSTSI GWTPPYSYTP
     LAADKVAADV KAKAGAGKI