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P11073

- PLYC_DICCH

UniProt

P11073 - PLYC_DICCH

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
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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 – 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

    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

    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.
    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

    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: October 1, 2014
    This is version 97 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