PTLY_BACLD
ID PTLY_BACLD Reviewed; 341 AA.
AC Q65DC2; Q62NU3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Pectate trisaccharide-lyase {ECO:0000250|UniProtKB:Q8GCB2};
DE EC=4.2.2.22;
DE AltName: Full=Exopolygalacturonate lyase {ECO:0000250|UniProtKB:Q8GCB2};
DE AltName: Full=Pectate lyase {ECO:0000250|UniProtKB:Q8GCB2, ECO:0000312|EMBL:AAU25568.1};
DE Flags: Precursor;
GN OrderedLocusNames=BLi04129, BL00947;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1] {ECO:0000312|EMBL:AAU25568.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
RN [2] {ECO:0000312|EMBL:AAU42942.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
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 (By similarity).
CC {ECO:0000250|UniProtKB:B1B6T1, ECO:0000250|UniProtKB:Q8GCB2}.
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:0000250|UniProtKB:Q8GCB2};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8GCB2};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000255}.
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DR EMBL; CP000002; AAU25568.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU42942.1; -; Genomic_DNA.
DR RefSeq; WP_003186388.1; NC_006322.1.
DR AlphaFoldDB; Q65DC2; -.
DR SMR; Q65DC2; -.
DR STRING; 279010.BL00947; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR EnsemblBacteria; AAU25568; AAU25568; BL00947.
DR GeneID; 66213933; -.
DR KEGG; bld:BLi04129; -.
DR KEGG; bli:BL00947; -.
DR eggNOG; COG3866; Bacteria.
DR HOGENOM; CLU_021894_2_1_9; -.
DR OMA; DNTQYVT; -.
DR OrthoDB; 660314at2; -.
DR BioCyc; BLIC279010:BLI_RS20305-MON; -.
DR Proteomes; UP000000606; Chromosome.
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 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Cell wall biogenesis/degradation; Lyase;
KW Metal-binding; Polysaccharide degradation; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..39
FT /evidence="ECO:0000250|UniProtKB:Q8GCB2, ECO:0000255"
FT /id="PRO_0000405010"
FT CHAIN 40..341
FT /note="Pectate trisaccharide-lyase"
FT /evidence="ECO:0000250|UniProtKB:Q8GCB2"
FT /id="PRO_0000405011"
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
