ID   PLYE1_DICCH             Reviewed;         385 AA.
AC   P04960;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Pectate lyase E;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   Name=pelE;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC16;
RX   PubMed=3536853; DOI=10.1128/jb.168.2.595-606.1986;
RA   Keen N.T., Tamaki S.;
RT   "Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and
RT   their high-level expression in Escherichia coli.";
RL   J. Bacteriol. 168:595-606(1986).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8081738; DOI=10.1016/0969-2126(93)90013-7;
RA   Yoder M.D., Lietzke S.E., Jurnak F.;
RT   "Unusual structural features in the parallel beta-helix in pectate
RT   lyases.";
RL   Structure 1:241-251(1993).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=12232373; DOI=10.1104/pp.106.3.849;
RA   Lietzke S.E., Yoder M.D., Keen N.T., Jurnak F.A.;
RT   "The three-dimensional structure of pectate lyase E, a plant virulence
RT   factor from Erwinia chrysanthemi.";
RL   Plant Physiol. 106:849-862(1994).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=12226275; DOI=10.1104/pp.111.1.73;
RA   Lietzke S.E., Scavetta R.D., Yoder M.D., Jurnak F.A.;
RT   "The refined three-dimensional structure of pectate lyase E from Erwinia
RT   chrysanthemi at 2.2-A resolution.";
RL   Plant Physiol. 111:73-92(1996).
CC   -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC       Note=Binds 1 Ca(2+) ion per subunit.;
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Pectate lyases have been implicated as pathogenicity
CC       factors which induce maceration or rotting of plant tissue. PelE is
CC       sufficient to induce these effects under laboratory conditions.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLBC
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M14509; AAA24844.1; -; Genomic_DNA.
DR   PIR; A25158; WZWC6E.
DR   RefSeq; WP_040000191.1; NZ_JAFCAF010000008.1.
DR   PDB; 1PCL; X-ray; 2.20 A; A=31-385.
DR   PDBsum; 1PCL; -.
DR   AlphaFoldDB; P04960; -.
DR   SMR; P04960; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   UniPathway; UPA00545; UER00824.
DR   EvolutionaryTrace; P04960; -.
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:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   3D-structure; Calcium; Lyase; Metal-binding; Repeat; Secreted; Signal.
FT   SIGNAL          1..30
FT   CHAIN           31..385
FT                   /note="Pectate lyase E"
FT                   /id="PRO_0000024857"
FT   REPEAT          177..182
FT                   /note="1"
FT   REPEAT          213..218
FT                   /note="2"
FT   REGION          177..218
FT                   /note="2 X 6 AA approximate repeats"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000255"
FT   BINDING         164
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  41250 MW;  23325AA3D5D810EA CRC64;
     MKNTRVRSIG TKSLLAAVVT AALMATSAYA AVETDAATTG WATQNGGTTG GAKAAKAVEV
     KNISDFKKAL NGTDSSAKII KVTGPIDISG GKAYTSFDDQ KARSQISIPS NTTIIGVGSN
     GKFTNGSLVI KGVKNVILRN LYIETPVDVA PHYESGDGWN AEWDAAVIDN STNVWVDHVT
     ISDGSFTDDK YTTKDGEKYV QHDGALDIKK GSDYVTISYS RFELHDKTIL IGHSDSNGSQ
     DSGKLRVTFH NNVFDRVTER APRVRFGSIH AYNNVYLGDV KHSVYPYLYS FGLGTSGSIL
     SESNSFTLSN LKSIDGKNPE CSIVKQFNSK VFSDKGSLVN GSTTTKLDTC GLTAYKPTLP
     YKYSAQTMTS SLATSINNNA GYGKL