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Protein

Pectate lyase C

Gene

pelC

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in maceration and soft-rotting of plant tissue.

Catalytic activityi

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.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi151 – 1511Calcium
Metal bindingi153 – 1531Calcium
Metal bindingi188 – 1881Calcium
Metal bindingi192 – 1921Calcium
Active sitei240 – 2401Sequence Analysis

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. pectate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
  2. pectin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Virulence

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectate lyase C (EC:4.2.2.2)
Gene namesi
Name:pelC
OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Taxonomic identifieri556 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 375353Pectate lyase CPRO_0000024854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi94 ↔ 177
Disulfide bondi351 ↔ 374

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
375
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 293Combined sources
Beta strandi41 – 477Combined sources
Helixi48 – 5710Combined sources
Beta strandi74 – 785Combined sources
Helixi83 – 908Combined sources
Helixi93 – 953Combined sources
Turni96 – 983Combined sources
Beta strandi103 – 1097Combined sources
Beta strandi113 – 1175Combined sources
Beta strandi123 – 1319Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi141 – 1444Combined sources
Helixi148 – 1503Combined sources
Beta strandi154 – 1596Combined sources
Beta strandi162 – 1676Combined sources
Beta strandi169 – 1713Combined sources
Helixi181 – 1833Combined sources
Beta strandi190 – 1967Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi206 – 2127Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi226 – 2316Combined sources
Beta strandi233 – 2397Combined sources
Beta strandi243 – 25311Combined sources
Beta strandi255 – 2617Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi271 – 2766Combined sources
Beta strandi278 – 28811Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi297 – 3026Combined sources
Helixi310 – 3145Combined sources
Helixi349 – 3557Combined sources
Helixi356 – 3583Combined sources
Beta strandi360 – 3645Combined sources
Helixi371 – 3733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP11073.
SMRiP11073. Positions 23-374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11073.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11073-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLITPITA GLLLALSQPL LAATDTGGYA ATAGGNVTGA VSKTATSMQD
60 70 80 90 100
IVNIIDAARL DANGKKVKGG AYPLVITYTG NEDSLINAAA ANICGQWSKD
110 120 130 140 150
PRGVEIKEFT KGITIIGANG SSANFGIWIK KSSDVVVQNM RIGYLPGGAK
160 170 180 190 200
DGDMIRVDDS PNVWVDHNEL FAANHECDGT PDNDTTFESA VDIKGASNTV
210 220 230 240 250
TVSYNYIHGV KKVGLDGSSS SDTGRNITYH HNYYNDVNAR LPLQRGGLVH
260 270 280 290 300
AYNNLYTNIT GSGLNVRQNG QALIENNWFE KAINPVTSRY DGKNFGTWVL
310 320 330 340 350
KGNNITKPAD FSTYSITWTA DTKPYVNADS WTSTGTFPTV AYNYSPVSAQ
360 370
CVKDKLPGYA GVGKNLATLT STACK
Length:375
Mass (Da):39,944
Last modified:July 1, 1989 - v1
Checksum:iF76DD8195A35B886
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19411 Genomic DNA. Translation: AAA24849.1.
PIRiA31091. WZWC6C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19411 Genomic DNA. Translation: AAA24849.1.
PIRiA31091. WZWC6C.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP11073.
SMRiP11073. Positions 23-374.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Miscellaneous databases

EvolutionaryTraceiP11073.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiPLYC_DICCH
AccessioniPrimary (citable) accession number: P11073
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.