ID   PLY_XANCM               Reviewed;         377 AA.
AC   Q56806;
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   AltName: Full=PSTRU-3;
DE   Flags: Precursor;
OS   Xanthomonas campestris pv. malvacearum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=86040;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B-414;
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}.
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; L38573; AAC41522.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q56806; -.
DR   SMR; Q56806; -.
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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..377
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024864"
FT   REGION          185..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000255"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
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"
SQ   SEQUENCE   377 AA;  40184 MW;  A947A0D9BF5A81A7 CRC64;
     MKPKFSTAAA ASLFVGSLLV VGVACADPAL EVATTGWATQ NGGTKGGSKA AAANIYTVKT
     AAELKSALKA SVGSNGRIIK ISGIIDVSEG KPYTTTSDMK SRARLDIPTK TTLIGITSNA
     EIREGYFYVK ANDVIIRNIT IENPWDPEPV WDPDDGSAGN WNSEYDGLTV EGATNVWVDH
     VTFTDGRRTD DQNGTANGRP KQHHDGAMDV KKGANFVTIS YSAFKSHEKN DLIGSSDSAS
     STDSGKLKVT IHNTLFENIS ARAPRVRFGQ VHLYNNYHVG STSNKVYPFS HAHGVGKESK
     IFSERNVFDI SGVSSCDKIA ADYGGSVYRD QGSLLNGKAL TCSWNSNIGW TPPYTYSLLS
     ADKVAADVKA KAGAGKL