ID   PLYP_YERPS              Reviewed;         572 AA.
AC   P11278; Q664D5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Periplasmic pectate lyase;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelY; OrderedLocusNames=YPTB3834;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ICBP 3821;
RX   PubMed=2832382; DOI=10.1128/jb.170.4.1825-1830.1988;
RA   Manulis S., Kobayashi D.Y., Keen N.T.;
RT   "Molecular cloning and sequencing of a pectate lyase gene from Yersinia
RT   pseudotuberculosis.";
RL   J. Bacteriol. 170:1825-1830(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA27660.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M19399; AAA27660.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BX936398; CAH23072.1; -; Genomic_DNA.
DR   PIR; A27742; WZEPPY.
DR   RefSeq; WP_002209555.1; NZ_CP009712.1.
DR   AlphaFoldDB; P11278; -.
DR   SMR; P11278; -.
DR   CAZy; PL2; Polysaccharide Lyase Family 2.
DR   EnsemblBacteria; CAH23072; CAH23072; YPTB3834.
DR   GeneID; 66843744; -.
DR   KEGG; ypo:BZ17_2750; -.
DR   KEGG; yps:YPTB3834; -.
DR   PATRIC; fig|273123.14.peg.2882; -.
DR   OMA; YPAGNEF; -.
DR   UniPathway; UPA00545; UER00824.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR010702; Pectate_lyase_2.
DR   Pfam; PF06917; Pectate_lyase_2; 1.
DR   PIRSF; PIRSF001432; Pect_lyase; 1.
PE   3: Inferred from homology;
KW   Lyase; Periplasm; Signal.
FT   SIGNAL          1..23
FT   CHAIN           24..572
FT                   /note="Periplasmic pectate lyase"
FT                   /id="PRO_0000024911"
SQ   SEQUENCE   572 AA;  64115 MW;  A01ADC208C2B5FB3 CRC64;
     MKKRALLLSM SVLAMLYIPA GQAAEIDRLT VVKQYVDNVL NKASDTYHGD KPSPLLADGV
     DPRTGQQMEW IFPDGRRAVL SNFSAQQNLM RVMSGLSELS GDPQYQKRAE DIVRYHFQNY
     QDNSGLLYWG GHRFVDLKTL QPEGPSEKEK VHELKNAYPY YDLMFSVDSD ATTRFIRGFW
     NAHVYDWRIL ETSRHGEYGK PMGALWESTF EQQPPFFATK GLSFLNAGND LIYSASLLYK
     YQQDQGALVW AKRLADQYVL PRDAKTGLGV YQFTQALKRE EPTDDADTHS KFGDRAQRQF
     GPEFGPTALE GNMMLKGRTS TLYSENALMQ LQLGKDLGGQ GDDLLKWTVD GLKAFAKYGY
     NEQDNTFRPM IANGQDLSNY TLPRDGYYGK KGSVLKPYKA GNEFLISYAR AYAVDNDPLL
     WKVARGIASD QGLGDIGSAP GKEMKVKLDT TNSDPYALFA LLDLYNASQV AEYRSLAEKV
     ADNIIKTRYI DGFFMASPDR QYADVDAIEP YALLALEASL RNKPQAVAPF LNGAGFTEGA
     YLMADGSARI STRDNELFLL NVGETLQPNG RK