ID   PLY_PSEMA               Reviewed;         380 AA.
AC   Q51915; Q53354;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Pectate lyase;
DE            Short=PL;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pel;
OS   Pseudomonas marginalis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=N6301;
RX   PubMed=7763884; DOI=10.1271/bbb.57.957;
RA   Nikaidou N., Kamio Y., Izaki K.;
RT   "Molecular cloning and nucleotide sequence of the pectate lyase gene from
RT   Pseudomonas marginalis N6301.";
RL   Biosci. Biotechnol. Biochem. 57:957-960(1993).
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; D32122; BAA06848.1; -; Genomic_DNA.
DR   EMBL; S65042; AAC60448.1; -; Genomic_DNA.
DR   PIR; JN0594; JN0594.
DR   AlphaFoldDB; Q51915; -.
DR   SMR; Q51915; -.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Lyase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..29
FT   CHAIN           30..380
FT                   /note="Pectate lyase"
FT                   /id="PRO_0000024861"
FT   REGION          189..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;  40812 MW;  FC1094904B997006 CRC64;
     MTKPSTFTAC KLASAVFGAL LFSSVPAHAA DIWLDVATTG WATQNGGTKG GSRAAANDIY
     TVKNAAELKK ALSASAGSNG RIIKITGIID VSEGKVYTKT ADMKVRGRLD IPGKTTIVGI
     GSNAEIREGF FYAKENDVII RNITVENPWD PEPIFDKDDG ADGNWNSEYD GLTVEGANNV
     WVDHVTFTDG RRTDDQNGTE HERPKQHHDG ALDVKNGANF VTISYSVFKS HEKNNLIGSS
     DSRTTDDGKL KVTIHNTLFE NISARAPRVR YGQVHLYNNY HVGSTSHKVY PFSYAHGVGK
     NSKIFSERNA FEIAGISGCD KIAGDYGGSV YRDTGSTLNG SALSCSWSSS IGWTPPYSYT
     PLAADKVAAD VKAKAGAGKL