ID   PLY_PSEFL               Reviewed;         380 AA.
AC   Q59671; Q51784;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Pectate lyase;
DE            Short=PL;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pel;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CY091 / Biovar 2;
RX   PubMed=8589419; DOI=10.1094/mpmi-9-0014;
RA   Liao C.H., Gaffney T.D., Bradley S.P., Wong L.C.;
RT   "Cloning of a pectate lyase gene from Xanthomonas campestris pv.
RT   malvacearum and comparison of its sequence relationship with pel genes of
RT   soft-rot Erwinia and Pseudomonas.";
RL   Mol. Plant Microbe Interact. 9:14-21(1996).
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; L38902; AAB46399.1; -; Genomic_DNA.
DR   EMBL; L41673; AAA93535.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59671; -.
DR   SMR; Q59671; -.
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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..380
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024860"
FT   REGION          191..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000255"
FT   BINDING         170
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  40624 MW;  ACDA387D0BC5DD95 CRC64;
     MTNPSTFTAS KLASAVIGAL LLSSVPAHAA DIWLDSATTG WATQNGGTKG GSRAAANNIY
     TAKNAAELKT ALKASVGANG RIIKITGIID ISEGKAYTTT ADMKVRGRLD IPGKTTIVGT
     TSNAEIREGF LYAKENDVII RNITIENPWD PEPKWDPTDG SAGNWNSEYD GLTIEGANNV
     WVDHVTFTDG RRTDDQNGTA NGRPKQHHDG ALDVKNGANY VTISYSAFKS HEKNNLIGSS
     DSRTTDDGKL KVTIHNTLFE NISARAPRVR FGQVHLYNNY HVGSTSHKVY PFSYAHGMGK
     NSKIFSERNA FEISGISGCD KIAGDYGGNV YRDTGSTVNG TALTCPWSTN IGWTPPYSYT
     PLAADKVAAD VKAKAGAGKL