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P11073

- PLYC_DICCH

UniProt

P11073 - PLYC_DICCH

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Protein

Pectate lyase C

Gene
pelC
Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed - 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

Binds 1 calcium 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 – 2401 Reviewed prediction

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 – 293
Beta strandi41 – 477
Helixi48 – 5710
Beta strandi74 – 785
Helixi83 – 908
Helixi93 – 953
Turni96 – 983
Beta strandi103 – 1097
Beta strandi113 – 1175
Beta strandi123 – 1319
Beta strandi134 – 1396
Beta strandi141 – 1444
Helixi148 – 1503
Beta strandi154 – 1596
Beta strandi162 – 1676
Beta strandi169 – 1713
Helixi181 – 1833
Beta strandi190 – 1967
Beta strandi199 – 2046
Beta strandi206 – 2127
Beta strandi215 – 2195
Beta strandi226 – 2316
Beta strandi233 – 2397
Beta strandi243 – 25311
Beta strandi255 – 2617
Beta strandi263 – 2675
Beta strandi271 – 2766
Beta strandi278 – 28811
Beta strandi290 – 2945
Beta strandi297 – 3026
Helixi310 – 3145
Helixi349 – 3557
Helixi356 – 3583
Beta strandi360 – 3645
Helixi371 – 3733

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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

MKSLITPITA GLLLALSQPL LAATDTGGYA ATAGGNVTGA VSKTATSMQD    50
IVNIIDAARL DANGKKVKGG AYPLVITYTG NEDSLINAAA ANICGQWSKD 100
PRGVEIKEFT KGITIIGANG SSANFGIWIK KSSDVVVQNM RIGYLPGGAK 150
DGDMIRVDDS PNVWVDHNEL FAANHECDGT PDNDTTFESA VDIKGASNTV 200
TVSYNYIHGV KKVGLDGSSS SDTGRNITYH HNYYNDVNAR LPLQRGGLVH 250
AYNNLYTNIT GSGLNVRQNG QALIENNWFE KAINPVTSRY DGKNFGTWVL 300
KGNNITKPAD FSTYSITWTA DTKPYVNADS WTSTGTFPTV AYNYSPVSAQ 350
CVKDKLPGYA GVGKNLATLT STACK 375
Length:375
Mass (Da):39,944
Last modified:July 1, 1989 - v1
Checksum:iF76DD8195A35B886
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19411 Genomic DNA. Translation: AAA24849.1.
PIRiA31091. WZWC6C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19411 Genomic DNA. Translation: AAA24849.1 .
PIRi A31091. WZWC6C.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AIR X-ray 2.20 A 23-375 [» ]
1O88 X-ray 2.20 A 23-375 [» ]
1O8D X-ray 2.20 A 23-375 [» ]
1O8E X-ray 2.20 A 23-375 [» ]
1O8F X-ray 2.20 A 23-375 [» ]
1O8G X-ray 2.20 A 23-375 [» ]
1O8H X-ray 2.20 A 23-375 [» ]
1O8I X-ray 2.20 A 23-375 [» ]
1O8J X-ray 2.20 A 23-375 [» ]
1O8K X-ray 2.20 A 23-375 [» ]
1O8L X-ray 2.20 A 23-375 [» ]
1O8M X-ray 2.20 A 23-375 [» ]
1PLU X-ray 2.20 A 23-375 [» ]
2EWE X-ray 2.20 A 23-375 [» ]
2PEC X-ray 2.20 A 23-375 [» ]
ProteinModelPortali P11073.
SMRi P11073. Positions 23-374.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi PL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00545 ; UER00824 .

Miscellaneous databases

EvolutionaryTracei P11073.

Family and domain databases

Gene3Di 2.160.20.10. 1 hit.
InterProi IPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view ]
Pfami PF00544. Pec_lyase_C. 1 hit.
[Graphical view ]
SMARTi SM00656. Amb_all. 1 hit.
[Graphical view ]
SUPFAMi SSF51126. SSF51126. 1 hit.
ProtoNeti Search...

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: April 16, 2014
This is version 96 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

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