PTLY_BACLI
ID PTLY_BACLI Reviewed; 341 AA.
AC Q8GCB2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Pectate trisaccharide-lyase;
DE EC=4.2.2.22;
DE AltName: Full=Exopolygalacturonate lyase {ECO:0000303|Ref.2};
DE AltName: Full=Pectate lyase A {ECO:0000303|PubMed:14673544, ECO:0000312|EMBL:CAD56882.1};
DE Short=PelA {ECO:0000303|PubMed:14673544};
DE Flags: Precursor;
GN Name=pelA {ECO:0000303|PubMed:14673544};
GN Synonyms=pel {ECO:0000312|EMBL:CAD56882.1};
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAD56882.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RC STRAIN=14A {ECO:0000269|PubMed:14673544};
RX PubMed=14673544; DOI=10.1007/s00253-003-1446-9;
RA Berensmeier S., Singh S.A., Meens J., Buchholz K.;
RT "Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical
RT characterization of recombinant, thermostable, high-alkaline pectate
RT lyase.";
RL Appl. Microbiol. Biotechnol. 64:560-567(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 40-57; 205-218 AND 243-249, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=14A {ECO:0000269|Ref.2};
RA Singh S.A., Plattner H., Diekmann H.;
RT "Exopolygalacturonate lyase from a thermophilic Bacillus sp.";
RL Enzyme Microb. Technol. 25:420-425(1999).
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:B1B6T1, ECO:0000269|PubMed:14673544,
CC ECO:0000269|Ref.2}.
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:14673544,
CC ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Inhibited by excess substrate. Inhibited by EDTA.
CC {ECO:0000269|PubMed:14673544, ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 11.0. Stable from pH 7.0 to 11.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 69 degrees Celsius. Thermostable, retains 100%
CC of activity after 2 hours incubation at 65 degrees Celsius.
CC {ECO:0000269|Ref.2};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000255}.
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DR EMBL; AJ517194; CAD56882.1; -; Genomic_DNA.
DR RefSeq; WP_003186388.1; NZ_VTQZ01000003.1.
DR AlphaFoldDB; Q8GCB2; -.
DR SMR; Q8GCB2; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR GeneID; 66213933; -.
DR PATRIC; fig|1402.62.peg.577; -.
DR BRENDA; 4.2.2.22; 669.
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|Ref.2"
FT /id="PRO_0000405012"
FT CHAIN 40..341
FT /note="Pectate trisaccharide-lyase"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000405013"
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"
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
