ID   PLYB_PAEAM              Reviewed;         391 AA.
AC   D3JTC2;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Pectate lyase B {ECO:0000303|PubMed:20622125};
DE            EC=4.2.2.2 {ECO:0000269|PubMed:20622125};
DE   AltName: Full=Pectin lyase {ECO:0000305|PubMed:20622125};
DE            EC=4.2.2.10 {ECO:0000269|PubMed:20622125};
DE   Flags: Precursor;
GN   Name=pelB {ECO:0000303|PubMed:20622125};
OS   Paenibacillus amylolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP   AND PATHWAY.
RC   STRAIN=27C64;
RX   PubMed=20622125; DOI=10.1128/aem.00043-10;
RA   Boland W.E., Henriksen E.D., Doran-Peterson J.;
RT   "Characterization of two Paenibacillus amylolyticus strain 27C64 pectate
RT   lyases with activity on highly methylated pectin.";
RL   Appl. Environ. Microbiol. 76:6006-6009(2010).
CC   -!- FUNCTION: Catalyzes the depolymerization of both polygalacturonate and
CC       pectins of various methyl esterification degree, with an endo mode of
CC       action. Shows the highest activity on 20 to 34% methylated pectin but
CC       retains 67%, 51%, 25%, and 1% of its maximum activity on
CC       polygalacturonate and 8.5%, 55 to 70%, and 90% methylated pectin,
CC       respectively. {ECO:0000269|PubMed:20622125}.
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         Evidence={ECO:0000269|PubMed:20622125};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC         ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC         galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC         Evidence={ECO:0000269|PubMed:20622125};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:20622125};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:20622125};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:20622125};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation.
CC       {ECO:0000269|PubMed:20622125}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20622125}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; GU289920; ADB78775.1; -; Genomic_DNA.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   BRENDA; 4.2.2.2; 632.
DR   UniPathway; UPA00545; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0030570; F:pectate lyase activity; IDA:UniProtKB.
DR   GO; GO:0047490; F:pectin lyase activity; IDA:UniProtKB.
DR   GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
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; 2.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Lyase; Metal-binding;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..391
FT                   /note="Pectate lyase B"
FT                   /id="PRO_5003047262"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000250|UniProtKB:P39116,
FT                   ECO:0000305|PubMed:20622125"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116,
FT                   ECO:0000305|PubMed:20622125"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116,
FT                   ECO:0000305|PubMed:20622125"
FT   BINDING         207
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P39116,
FT                   ECO:0000305|PubMed:20622125"
SQ   SEQUENCE   391 AA;  42204 MW;  B1D6934BA705F5CC CRC64;
     MKKTVRSLCS TALALTLGFT LLSGPASVQA AGNADYNLAG FSQGNTGGGI ISESNTSTYK
     KVYNATDLAL ALKKNSGVKV VEIMNDLDLG WNEIPSAAQT SPFAKHNDAL THPVLKQTGV
     SKITVDGFNG LTIFSANGSK IKHAAITVKR SSNVIIRNLE FDELWEWDES TKGDYDKNDW
     DYITLEDSSG VWIDHCTFNK AYDGLVDSKK GTSGVTISWS TFKGDDGSAN SWVTRQINEL
     EANKASYPMY NYLRSSAVGL SKQDVIAISG PQKKGHLVGA TSLESANANL SITLHHNLYK
     DIQDRMPRLR GGNAHAYNII MDAADARSAQ SRITSAMATA IASKGYKFGI TSNGAISTES
     GAVLVEKSVI KDVQXPCTQQ SDRSDQRHVH R