PLY1_PECAS
ID PLY1_PECAS Reviewed; 374 AA.
AC Q6CZT4; P11430; P16529; Q06113; Q47468;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Pectate lyase 1;
DE EC=4.2.2.2;
DE AltName: Full=Pectate lyase A;
DE Short=PLA;
DE AltName: Full=Pectate lyase I;
DE Short=PEL I;
DE Flags: Precursor;
GN Name=pel1; Synonyms=pelA; OrderedLocusNames=ECA4067;
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 PROTEIN SEQUENCE OF 23-36.
RC STRAIN=EC;
RX PubMed=3371662; DOI=10.1016/0378-1119(88)90590-2;
RA Lei S.-P., Lin H.-C., Wang S.-S., Wilcox G.;
RT "Characterization of the Erwinia carotovora pelA gene and its product
RT pectate lyase A.";
RL Gene 62:159-164(1988).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA24845.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M18859; AAA24845.1; ALT_INIT; Genomic_DNA.
DR EMBL; X81847; CAA57439.1; -; Genomic_DNA.
DR EMBL; BX950851; CAG76964.1; -; Genomic_DNA.
DR PIR; JT0242; WZWCP1.
DR RefSeq; WP_011095541.1; NC_004547.2.
DR AlphaFoldDB; Q6CZT4; -.
DR SMR; Q6CZT4; -.
DR STRING; 218491.ECA4067; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR EnsemblBacteria; CAG76964; CAG76964; ECA4067.
DR GeneID; 57210731; -.
DR KEGG; eca:ECA4067; -.
DR PATRIC; fig|218491.5.peg.4135; -.
DR eggNOG; COG3866; Bacteria.
DR HOGENOM; CLU_021894_2_1_6; -.
DR OMA; DSADCIC; -.
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 /evidence="ECO:0000269|PubMed:3371662"
FT CHAIN 23..374
FT /note="Pectate lyase 1"
FT /id="PRO_0000234448"
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 13
FT /note="L -> V (in Ref. 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..66
FT /note="VDIIEAAKKDSSGKVV -> INLIEEAQLDSKGKKL (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="V -> A (in Ref. 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="F -> Y (in Ref. 1; AAA24845 and 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="I -> L (in Ref. 1; AAA24845)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> L (in Ref. 1; AAA24845)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> M (in Ref. 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="V -> I (in Ref. 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="I -> V (in Ref. 1; AAA24845)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> G (in Ref. 1; AAA24845)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="F -> Y (in Ref. 1; AAA24845 and 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Y -> H (in Ref. 1; AAA24845)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="Y -> H (in Ref. 1; AAA24845)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="N -> T (in Ref. 1; AAA24845)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="D -> G (in Ref. 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="K -> N (in Ref. 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> P (in Ref. 1; AAA24845 and 2; CAA57439)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="N -> S (in Ref. 2; CAA57439)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 40178 MW; DDDA152B0F49CDDA CRC64;
MKYLLPSAAA GLLLLAAQPT MAANTGGYAT TDGGDVSGAV KKTARSLQEI VDIIEAAKKD
SSGKVVKGGA FPLVITYNGN EDALIKAAEA NICGQWSKDP RGVEIKEFTK GITILGTNGS
SANFGIWVVN SSNVVVRNMR FGYMPGGAKD GDAIRIDNSP NVWIDHNEIF AKNFECAGTP
DNDTTFESAV DIKKASTNVT VSYNFIHGVK KVGLSGSSNT DTGRNLTYHH NIYSDVNSRL
PLQRGGQVHA YNNLYDGIKS SGFNVRQKGI ALIESNWFEN ALNPVTARND DSNFGTWELR
NNNITSPSDF AKYKITWGKP STPHINADDW KSTGKFPAVS YSYSPVSAQC VKDKLANYAG
VGKNQAVLTA ANCK
