ID   PLY_PSEVI               Reviewed;         380 AA.
AC   Q60140; Q52619;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Pectate lyase;
DE            Short=PL;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pel;
OS   Pseudomonas viridiflava.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=33069;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SJ074;
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; L38901; AAB46398.1; -; Genomic_DNA.
DR   EMBL; D44611; BAA08077.1; -; Genomic_DNA.
DR   EMBL; L38574; AAC41521.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q60140; -.
DR   SMR; Q60140; -.
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..380
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024863"
FT   REGION          189..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"
FT   CONFLICT        297
FT                   /note="I -> V (in Ref. 1; AAC41521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="L -> DSRGS (in Ref. 1; AAC41521)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  40384 MW;  BB4ABC2B715D51C6 CRC64;
     MVKPSLFSAN KLASAVVASL LFASAGAQAD IATDVATTGW ATQNGGTKGG SKAAANNIYT
     VKNAAELKAA LKASVGTNGR IIKISGVIDV SEGNAYTKTA DMKARGRLDI PGKTTIVGIT
     NNAEIREGFF YAKENDVIIR NLTIENPWDP EPIWDANDGS AGNWNSEYDG LTIEGANNVW
     VDHVTFTDGR RTDDQNGTAN GRPKQHHDGA LDVKNGANYV TISYTAFKSH EKNNLIGSSD
     SRTTDDGKLK VTIHNSLFEN ISARAPRVRF GQVHLYNNYH VGSASHSVYP FSYAHGIGKS
     SKIFSEKNAF EISGISGCTK IAGDYGGSVY RDSGSTLNGT ALTCTWSSSI GWTPPYSYTP
     LNADKVKADV TAKAGAGKIL