ID   PLYP_PECCC              Reviewed;         568 AA.
AC   P14005;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Periplasmic pectate lyase;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelB;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=2695748; DOI=10.1111/j.1365-2958.1989.tb00164.x;
RA   Hinton J.C.D., Sidebotham J.M., Gill D.R., Salmond G.P.C.;
RT   "Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia
RT   carotovora subspecies carotovora belong to different gene families.";
RL   Mol. Microbiol. 3:1785-1795(1989).
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}.
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DR   EMBL; X16397; CAA34432.1; -; Genomic_DNA.
DR   PIR; S07653; WZWCCC.
DR   RefSeq; WP_039473295.1; NZ_JUJS01000001.1.
DR   AlphaFoldDB; P14005; -.
DR   SMR; P14005; -.
DR   CAZy; PL2; Polysaccharide Lyase Family 2.
DR   UniPathway; UPA00545; UER00824.
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..19
FT   CHAIN           20..568
FT                   /note="Periplasmic pectate lyase"
FT                   /id="PRO_0000024910"
SQ   SEQUENCE   568 AA;  63524 MW;  23B88CB34528F8CB CRC64;
     MKRFALSLLA GLVALQASAA TPDRLTIVNQ YVDNVLTKAG DHYHGQSPTP LLADGVDPRT
     GKQMEWIFPD GRHAVLSNFS AQQNLMRVLV GLSNLSGNPS YKQRAEAIVK YHFQHYQDES
     GLLIWGGHRF VDLKTLQPEG PSEKEMVHEL KNAYPYYDLM FSVDKDATAR FIRGFWNAHV
     YDWKIMETSR HGKYGQKIGA LWQSPFEQQP PFFATKGLSF LNAGNDLIYS ASLLYKYNKE
     DGALVWAKRL AQQYVLPRDK ATGLGVYQFT QALKRDETTD DADTHSKYGD RAQRQFGPEF
     GPTALEGNMM LKGRTSTIYS ENALMQLQLG KDLGAEGKEL LTWTTDGLKA FAKYAYNESD
     NTFRPMLANG KDLSNYVLPR DGYYGKKGTV IKPYPADNSF LLSYARAYTV LPDAELWRVA
     RGIARAQGLG ELGSAPGKDV KVDLATKNND PYALFALLDL YQASKVKDYL SLAEKVGDNI
     ISTRYQNGFF MAEPNRQYAD VDTIEPYALL ALEAAVRNQP QSVAPFLNGA GFTEGGYRME
     DGSTRVSTRD NEIFLLNVGE TLKPNNKK