ID   PLYC_BACSU              Reviewed;         221 AA.
AC   O34310; Q795F2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=BSU34950;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT   "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT   subtilis.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   GENE NAME, FUNCTION, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=168;
RX   PubMed=16514142; DOI=10.1099/mic.0.28562-0;
RA   Soriano M., Diaz P., Pastor F.I.J.;
RT   "Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with
RT   activity on highly methylated pectin.";
RL   Microbiology 152:617-625(2006).
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. Is also able to cleave
CC       trigalacturonate to galacturonic acid and unsaturated digalacturonate.
CC       {ECO:0000269|PubMed:16514142}.
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;
CC         Evidence={ECO:0000269|PubMed:16514142};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:16514142};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=256.7 umol/min/mg enzyme with 22% esterified pectin as substrate
CC         {ECO:0000269|PubMed:16514142};
CC         Vmax=59.6 umol/min/mg enzyme with polygalacturonic acid as substrate
CC         {ECO:0000269|PubMed:16514142};
CC       pH dependence:
CC         Optimum pH is 10. {ECO:0000269|PubMed:16514142};
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius. Thermostable at 50 degrees
CC         Celsius in buffers at pH 7. {ECO:0000269|PubMed:16514142};
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   -!- MISCELLANEOUS: Hg(2+) could replace calcium ion.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AF017113; AAC67291.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15500.1; -; Genomic_DNA.
DR   PIR; A70045; A70045.
DR   RefSeq; NP_391375.1; NC_000964.3.
DR   RefSeq; WP_003242578.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O34310; -.
DR   SMR; O34310; -.
DR   STRING; 224308.BSU34950; -.
DR   CAZy; PL3; Polysaccharide Lyase Family 3.
DR   PaxDb; O34310; -.
DR   EnsemblBacteria; CAB15500; CAB15500; BSU_34950.
DR   GeneID; 936594; -.
DR   KEGG; bsu:BSU34950; -.
DR   PATRIC; fig|224308.179.peg.3783; -.
DR   eggNOG; COG5297; Bacteria.
DR   InParanoid; O34310; -.
DR   OMA; IFQINKA; -.
DR   PhylomeDB; O34310; -.
DR   BioCyc; BSUB:BSU34950-MON; -.
DR   UniPathway; UPA00545; UER00824.
DR   Proteomes; UP000001570; 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   1: Evidence at protein level;
KW   Calcium; Lyase; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..221
FT                   /note="Pectate lyase C"
FT                   /id="PRO_0000233104"
SQ   SEQUENCE   221 AA;  24281 MW;  AB324700DE573236 CRC64;
     MKKIVSILFM FGLVMGFSQF QPSTVFAADK VVHETIIVPK NTTYDGKGQR FVAGKELGDG
     SQSENQDPVF RVEDGATLKN VVLGAPAADG VHTYGNVNIQ NVKWEDVGED ALTVKKEGKV
     TIDGGSAQKA SDKIFQINKA STFTVKNFTA DNGGKFIRQL GGSTFHVDVI IDKCTITNMK
     EAIFRTDSKT STVRMTNTRY SNVGQKWIGV QHIYENNNTQ F