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Q6CZT3 (PLY2_ERWCT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pectate lyase 2
EC=4.2.2.2
Alternative name(s):
Pectate lyase B
Short name=PLB
Pectate lyase II
Short name=PEL II
Gene names
Name:pel2
Synonyms:pelB
Ordered Locus Names:ECA4068
OrganismErwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]
Taxonomic identifier29471 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in maceration and soft-rotting of plant tissue.

Catalytic activity

Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.

Subcellular location

Secreted.

Sequence similarities

Belongs to the polysaccharide lyase 1 family. PLADES subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 374352Pectate lyase 2
PRO_0000234449

Sites

Active site2391 Potential
Metal binding1501Calcium By similarity
Metal binding1521Calcium By similarity
Metal binding1871Calcium By similarity
Metal binding1911Calcium By similarity

Amino acid modifications

Disulfide bond93 ↔ 176 By similarity
Disulfide bond350 ↔ 373 By similarity

Experimental info

Sequence conflict101T → A in AAA24848. Ref.1
Sequence conflict101T → A in CAA57440. Ref.2
Sequence conflict211V → M in AAA24848. Ref.1
Sequence conflict211V → M in CAA57440. Ref.2
Sequence conflict351E → D in AAA24848. Ref.1
Sequence conflict361T → V in AAA24848. Ref.1
Sequence conflict361T → V in CAA57440. Ref.2
Sequence conflict47 – 482LQ → MK in CAA57440. Ref.2
Sequence conflict581K → Q in CAA57440. Ref.2
Sequence conflict781N → S in CAA57440. Ref.2
Sequence conflict1151L → Q in AAA24848. Ref.1
Sequence conflict1151L → Q in CAA57440. Ref.2
Sequence conflict1331D → N in AAA24848. Ref.1
Sequence conflict1331D → N in CAA57440. Ref.2
Sequence conflict1361V → L in CAA57440. Ref.2
Sequence conflict1391M → I in CAA57440. Ref.2
Sequence conflict1441M → I in CAA57440. Ref.2
Sequence conflict1501D → H in CAA57440. Ref.2
Sequence conflict1561V → I in CAA57440. Ref.2
Sequence conflict1681E → K in AAA24848. Ref.1
Sequence conflict172 – 1732KN → QS in AAA24848. Ref.1
Sequence conflict2341R → S in CAA57440. Ref.2
Sequence conflict2521N → T in AAA24848. Ref.1
Sequence conflict2801N → I in AAA24848. Ref.1
Sequence conflict3041V → I in AAA24848. Ref.1
Sequence conflict3041V → I in CAA57440. Ref.2
Sequence conflict3141N → K in CAA57440. Ref.2
Sequence conflict3191R → K in CAA57440. Ref.2
Sequence conflict3221T → S in CAA57440. Ref.2
Sequence conflict3251V → I in CAA57440. Ref.2
Sequence conflict3321N → S in AAA24848. Ref.1
Sequence conflict3321N → S in CAA57440. Ref.2
Sequence conflict338 – 3392SI → AV in CAA57440. Ref.2
Sequence conflict3441S → T Ref.1
Sequence conflict3441S → T Ref.2
Sequence conflict3621S → G Ref.1
Sequence conflict3621S → G Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6CZT3 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 2F8C41B4C30DA91B

FASTA37440,446
        10         20         30         40         50         60 
MKYLLPTAAT GLLLLAAQPA VAANTGGYAT TDGGETSGAV KKTARSLQEI VDIIEAAKVD 

        70         80         90        100        110        120 
SKGKKVKGGA YPLIITYNGN EDSLIKAAEK NICGQWSKDA RGVQIKEFTK GITILGTNGS 

       130        140        150        160        170        180 
SANFGVWIVN SSDVVVRNMR FGYMPGGAQD GDAIRVDNSP NVWIDHNEIF AKNFECKGTP 

       190        200        210        220        230        240 
DNDTTFESAV DIKKGSTNVT VSYNYIHGIK KVGLSGASNT DTGRNLTYHH NIYRDVNSRL 

       250        260        270        280        290        300 
PLQRGGLVHA YNNLYDGITG SGFNVRQKGI ALIESNWFEN ALNPVTARND SSNFGTWELR 

       310        320        330        340        350        360 
NNNVTKPADF SKYNITWGRP STPHVNADDW KNTGKFPSIS YKYSPVSAQC VKDKLANYAG 

       370 
VSKNLAVLTA ANCK

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the Erwinia carotovora pelB gene and its product pectate lyase."
Lei S.-P., Lin H.-C., Wang S.-S., Callaway J., Wilcox G.
J. Bacteriol. 169:4379-4383(1987) [PubMed: 3040692] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: EC.
[2]"Synergism between Erwinia pectate lyase isoenzymes that depolymerize both pectate and pectin."
Bartling S., Wegener C., Olsen O.
Microbiology 141:873-881(1995) [PubMed: 7773390] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C18.
[3]"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors."
Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. expand/collapse author list , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.
Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M17364 Genomic DNA. Translation: AAA24848.1.
X81847 Genomic DNA. Translation: CAA57440.1.
BX950851 Genomic DNA. Translation: CAG76965.1.
RefSeqYP_052155.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6CZT3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2885351.
GenomeReviewsGene locus ECA4068 in contig BX950851_GR.
KEGGeca:ECA4068.
NMPDRfig|218491.3.peg.2899.
PATRIC20483583. VBIPecAtr54885_4137.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG401253.
OMANGNEDSL.
ProtClustDBCLSK2307645.

Enzyme and pathway databases

BioCycECAR218491:ECA4068-MONOMER.

Family and domain databases

InterProIPR002022. Amb_allergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
KOK01728.
PfamPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLY2_ERWCT
AccessionPrimary (citable) accession number: Q6CZT3
Secondary accession number(s): P11431, Q06112, Q47469
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: August 16, 2004
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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