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P11073 (PLYC_DICCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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 C

EC=4.2.2.2
Gene names
Name:pelC
OrganismDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic identifier556 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length375 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.

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
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

pectin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 375353Pectate lyase C
PRO_0000024854

Sites

Active site2401 Potential
Metal binding1511Calcium
Metal binding1531Calcium
Metal binding1881Calcium
Metal binding1921Calcium

Amino acid modifications

Disulfide bond94 ↔ 177
Disulfide bond351 ↔ 374

Secondary structure

.................................................................... 375
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11073 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: F76DD8195A35B886

FASTA37539,944
        10         20         30         40         50         60 
MKSLITPITA GLLLALSQPL LAATDTGGYA ATAGGNVTGA VSKTATSMQD IVNIIDAARL 

        70         80         90        100        110        120 
DANGKKVKGG AYPLVITYTG NEDSLINAAA ANICGQWSKD PRGVEIKEFT KGITIIGANG 

       130        140        150        160        170        180 
SSANFGIWIK KSSDVVVQNM RIGYLPGGAK DGDMIRVDDS PNVWVDHNEL FAANHECDGT 

       190        200        210        220        230        240 
PDNDTTFESA VDIKGASNTV TVSYNYIHGV KKVGLDGSSS SDTGRNITYH HNYYNDVNAR 

       250        260        270        280        290        300 
LPLQRGGLVH AYNNLYTNIT GSGLNVRQNG QALIENNWFE KAINPVTSRY DGKNFGTWVL 

       310        320        330        340        350        360 
KGNNITKPAD FSTYSITWTA DTKPYVNADS WTSTGTFPTV AYNYSPVSAQ CVKDKLPGYA 

       370 
GVGKNLATLT STACK 

« Hide

References

[1]"Structure and organization of the pel genes from Erwinia chrysanthemi EC16."
Tamaki S.J., Gold S., Robeson M., Manulis S., Keen N.T.
J. Bacteriol. 170:3468-3478(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: EC16.
[2]"New domain motif: the structure of pectate lyase C, a secreted plant virulence factor."
Yoder M.D., Keen N.T., Jurnak F.
Science 260:1503-1507(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[3]"The refined three-dimensional structure of pectate lyase E from Erwinia chrysanthemi at 2.2-A resolution."
Lietzke S.E., Scavetta R.D., Yoder M.D., Jurnak F.A.
Plant Physiol. 111:73-92(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]"Characterization and implications of Ca2+ binding to pectate lyase C."
Herron S.R., Scavetta R.D., Garrett M., Legner M., Jurnak F.
J. Biol. Chem. 278:12271-12277(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19411 Genomic DNA. Translation: AAA24849.1.
PIRWZWC6C. A31091.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIRX-ray2.20A23-375[»]
1O88X-ray2.20A23-375[»]
1O8DX-ray2.20A23-375[»]
1O8EX-ray2.20A23-375[»]
1O8FX-ray2.20A23-375[»]
1O8GX-ray2.20A23-375[»]
1O8HX-ray2.20A23-375[»]
1O8IX-ray2.20A23-375[»]
1O8JX-ray2.20A23-375[»]
1O8KX-ray2.20A23-375[»]
1O8LX-ray2.20A23-375[»]
1O8MX-ray2.20A23-375[»]
1PLUX-ray2.20A23-375[»]
2EWEX-ray2.20A23-375[»]
2PECX-ray2.20A23-375[»]
ProteinModelPortalP11073.
SMRP11073. Positions 23-374.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00545; UER00824.

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMSSF51126. SSF51126. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP11073.

Entry information

Entry namePLYC_DICCH
AccessionPrimary (citable) accession number: P11073
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways