ID   PTLY_BACSP              Reviewed;         341 AA.
AC   B1B6T1;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Pectate trisaccharide-lyase;
DE            EC=4.2.2.22;
DE   AltName: Full=Exopolygalacturonate lyase {ECO:0000250|UniProtKB:Q8GCB2};
DE   AltName: Full=Pectate lyase {ECO:0000303|PubMed:19202269, ECO:0000312|EMBL:BAG12908.1};
DE   AltName: Full=Pel SWU {ECO:0000303|PubMed:19202269};
DE   Flags: Precursor;
GN   Name=pel {ECO:0000312|EMBL:BAG12908.1};
OS   Bacillus sp.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1409;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAG12908.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-64 AND 144-161,
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=RN1 {ECO:0000312|EMBL:BAG12908.1};
RX   PubMed=19202269; DOI=10.1271/bbb.80287;
RA   Sukhumsiirchart W., Kawanishi S., Deesukon W., Chansiri K., Kawasaki H.,
RA   Sakamoto T.;
RT   "Purification, characterization, and overexpression of thermophilic pectate
RT   lyase of Bacillus sp. RN1 isolated from a hot spring in Thailand.";
RL   Biosci. Biotechnol. Biochem. 73:268-273(2009).
CC   -!- FUNCTION: Cleaves unsaturated oligo-galacturonides from pectin. The
CC       major product is trigalacturonate; digalacturonate and
CC       tetragalacturonate are also produced. Activity on methylated pectins
CC       decreases with an increasing degree of methylation.
CC       {ECO:0000250|UniProtKB:Q8GCB2, ECO:0000269|PubMed:19202269}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eliminative cleavage of unsaturated trigalacturonate as the
CC         major product from the reducing end of polygalacturonic
CC         acid/pectate.; EC=4.2.2.22; Evidence={ECO:0000269|PubMed:19202269};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q8GCB2};
CC   -!- ACTIVITY REGULATION: Completely inhibited by EDTA. Activated by 0.5 mM
CC       MgCl(2), slightly activated by 0.5 mM BaCl(2) and 0.5 mM MnCl(2).
CC       Partially inhibited by 0.5 mM CoCl(2), 0.5 mM NiCl(2) and 0.5 mM
CC       ZnCl(2). Activity is maximal in the presence of 0.5 mM CaCl(2), and
CC       decreases gradually at higher concentrations.
CC       {ECO:0000269|PubMed:19202269}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000255}.
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DR   EMBL; AB428424; BAG12908.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1B6T1; -.
DR   SMR; B1B6T1; -.
DR   PRIDE; B1B6T1; -.
DR   BRENDA; 4.2.2.2; 691.
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:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Lyase; Metal-binding;
KW   Polysaccharide degradation; Repeat; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..39
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:19202269"
FT                   /id="PRO_0000405014"
FT   CHAIN           40..341
FT                   /note="Pectate trisaccharide-lyase"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GCB2"
FT                   /id="PRO_0000405015"
FT   REPEAT          131..156
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          158..186
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          262..283
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          287..322
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
FT   BINDING         150
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
FT   BINDING         180
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116"
FT   CONFLICT        161
FT                   /note="I -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   341 AA;  37365 MW;  4662DFCBF915E9C6 CRC64;
     MKKLISIIFI FVLGVVGSLT AAVSAEAASA LNSGKVNPLA DFSLKGFAAL NGGTTGGEGG
     QTVTVTTGDQ LIAALKNKNA NTPLKIYVNG TITTSNTSAS KIDVKDVSNV SIVGSGTKGE
     LKGIGIKIWR ANNIIIRNLK IHEVASGDKD AIGIEGPSKN IWVDHNELYH SLNVDKDYYD
     GLFDVKRDAE YITFSWNYVH DGWKSMLMGS SDSDNYNRTI TFHHNWFENL NSRVPSFRFG
     EGHIYNNYFN KIIDSGINSR MGARIRIENN LFENAKDPIV SWYSSSPGYW HVSNNKFVNS
     RGSMPTTSTT TYNPPYSYSL DNVDNVKSIV KQNAGVGKIN P