PLY2_PECAS
ID PLY2_PECAS Reviewed; 374 AA.
AC Q6CZT3; P11431; Q06112; Q47469;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Pectate lyase 2;
DE EC=4.2.2.2;
DE AltName: Full=Pectate lyase B;
DE Short=PLB;
DE AltName: Full=Pectate lyase II;
DE Short=PEL II;
DE Flags: Precursor;
GN Name=pel2; Synonyms=pelB; OrderedLocusNames=ECA4068;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=EC;
RX PubMed=3040692; DOI=10.1128/jb.169.9.4379-4383.1987;
RA Lei S.-P., Lin H.-C., Wang S.-S., Callaway J., Wilcox G.;
RT "Characterization of the Erwinia carotovora pelB gene and its product
RT pectate lyase.";
RL J. Bacteriol. 169:4379-4383(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C18;
RX PubMed=7773390; DOI=10.1099/13500872-141-4-873;
RA Bartling S., Wegener C., Olsen O.;
RT "Synergism between Erwinia pectate lyase isoenzymes that depolymerize both
RT pectate and pectin.";
RL Microbiology 141:873-881(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; 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.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. PLADES
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M17364; AAA24848.1; -; Genomic_DNA.
DR EMBL; X81847; CAA57440.1; -; Genomic_DNA.
DR EMBL; BX950851; CAG76965.1; -; Genomic_DNA.
DR RefSeq; WP_011095542.1; NC_004547.2.
DR AlphaFoldDB; Q6CZT3; -.
DR SMR; Q6CZT3; -.
DR STRING; 218491.ECA4068; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR EnsemblBacteria; CAG76965; CAG76965; ECA4068.
DR GeneID; 57210732; -.
DR KEGG; eca:ECA4068; -.
DR PATRIC; fig|218491.5.peg.4137; -.
DR eggNOG; COG3866; Bacteria.
DR HOGENOM; CLU_021894_2_1_6; -.
DR OMA; DNTQYVT; -.
DR OrthoDB; 660314at2; -.
DR UniPathway; UPA00545; UER00824.
DR Proteomes; UP000007966; 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: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 Calcium; Direct protein sequencing; Disulfide bond; Lyase; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT CHAIN 23..374
FT /note="Pectate lyase 2"
FT /id="PRO_0000234449"
FT ACT_SITE 239
FT /evidence="ECO:0000255"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 93..176
FT /evidence="ECO:0000250"
FT DISULFID 350..373
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="T -> A (in Ref. 1; AAA24848 and 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="V -> M (in Ref. 1; AAA24848 and 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="E -> D (in Ref. 1; AAA24848)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="T -> V (in Ref. 1; AAA24848 and 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..48
FT /note="LQ -> MK (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="K -> Q (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="N -> S (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="L -> Q (in Ref. 1; AAA24848 and 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="D -> N (in Ref. 1; AAA24848 and 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="V -> L (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="M -> I (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="M -> I (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> H (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="V -> I (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="E -> K (in Ref. 1; AAA24848)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..173
FT /note="KN -> QS (in Ref. 1; AAA24848)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="R -> S (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="N -> T (in Ref. 1; AAA24848)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="N -> I (in Ref. 1; AAA24848)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="V -> I (in Ref. 1; AAA24848 and 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="N -> K (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="R -> K (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="T -> S (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="V -> I (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="N -> S (in Ref. 1; AAA24848 and 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..339
FT /note="SI -> AV (in Ref. 2; CAA57440)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="S -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 40446 MW; 2F8C41B4C30DA91B CRC64;
MKYLLPTAAT GLLLLAAQPA VAANTGGYAT TDGGETSGAV KKTARSLQEI VDIIEAAKVD
SKGKKVKGGA YPLIITYNGN EDSLIKAAEK NICGQWSKDA RGVQIKEFTK GITILGTNGS
SANFGVWIVN SSDVVVRNMR FGYMPGGAQD GDAIRVDNSP NVWIDHNEIF AKNFECKGTP
DNDTTFESAV DIKKGSTNVT VSYNYIHGIK KVGLSGASNT DTGRNLTYHH NIYRDVNSRL
PLQRGGLVHA YNNLYDGITG SGFNVRQKGI ALIESNWFEN ALNPVTARND SSNFGTWELR
NNNVTKPADF SKYNITWGRP STPHVNADDW KNTGKFPSIS YKYSPVSAQC VKDKLANYAG
VSKNLAVLTA ANCK
