ID   PLYC_BACLD              Reviewed;         221 AA.
AC   Q65EF5; Q62PX3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Pectate lyase C;
DE            EC=4.2.2.2;
DE   AltName: Full=Pectin lyase;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelC; Synonyms=yvpA; OrderedLocusNames=BLi03741, BL03597;
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]
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).
RN   [2]
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).
CC   -!- FUNCTION: Catalyzes the depolymerization of both polygalacturonate and
CC       pectins of methyl esterification degree from 22 to 89%, with an endo
CC       mode of action. In contrast to the majority of pectate lyases, displays
CC       high activity on highly methylated pectins (By similarity).
CC       {ECO:0000250}.
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   -!- 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   -!- 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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU42559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017333; AAU42559.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000002; AAU25188.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q65EF5; -.
DR   SMR; Q65EF5; -.
DR   STRING; 279010.BL03597; -.
DR   CAZy; PL3; Polysaccharide Lyase Family 3.
DR   EnsemblBacteria; AAU25188; AAU25188; BL03597.
DR   KEGG; bld:BLi03741; -.
DR   KEGG; bli:BL03597; -.
DR   PATRIC; fig|279010.13.peg.3806; -.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_044863_3_1_9; -.
DR   OMA; IFQINKA; -.
DR   UniPathway; UPA00545; UER00824.
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:UniProtKB-EC.
DR   GO; GO:0047490; F:pectin 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; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR33407; PTHR33407; 1.
DR   Pfam; PF03211; Pectate_lyase; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Calcium; Lyase; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..221
FT                   /note="Pectate lyase C"
FT                   /id="PRO_0000233103"
SQ   SEQUENCE   221 AA;  23618 MW;  B15454293DC27FC4 CRC64;
     MKRLAGTVIL SGLLVCGFGQ ALPEKALAAE VVHKTIVVEK GQTYDGKGKR LIAGPELGDG
     SQREDQKPIF KVEDGATLKN VVLGAPAADG VHTYGNASIN NVVWEDVGED ALTVKSEGSV
     TINGGSARLA ADKIFQINKA STFTVKNFTA DQGGKFIRQL GGSTFKAVVN IDNCTITNMK
     EAIFRTDSST SSVTMTNTRY SKVGQKWIGV KHATERNNHE F