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B1B6T1 (PTLY_BACSP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pectate trisaccharide-lyase
EC=4.2.2.22
Alternative name(s):
Exopolygalacturonate lyase
Pectate lyase
Pel SWU
Gene names
Name:pel
OrganismBacillus sp.
Taxonomic identifier1409 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves unsaturated oligo-galacturonides from pectin. The major product is trigalacturonate; digalacturonate and tetragalacturonate are also produced. Activity on methylated pectins decreases with an increasing degree of methylation. Ref.1 UniProtKB Q8GCB2

Catalytic activity

Eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate. Ref.1

Cofactor

Calcium By similarity. UniProtKB Q8GCB2

Enzyme regulation

Completely inhibited by EDTA. Activated by 0.5 mM MgCl2, slightly activated by 0.5 mM BaCl2 and 0.5 mM MnCl2. Partially inhibited by 0.5 mM CoCl2, 0.5 mM NiCl2 and 0.5 mM ZnCl2. Activity is maximal in the presence of 0.5 mM CaCl2, and decreases gradually at higher concentrations. Ref.1

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the polysaccharide lyase 1 family.

Contains 4 PbH1 repeats.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionlyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 3912 UniProtKB Q8GCB2
PRO_0000405014
Chain40 – 341302Pectate trisaccharide-lyase UniProtKB Q8GCB2
PRO_0000405015

Regions

Repeat131 – 15626PbH1 1
Repeat158 – 18629PbH1 2
Repeat262 – 28322PbH1 3
Repeat287 – 32236PbH1 4

Sites

Active site2331 By similarity UniProtKB P39116
Metal binding1501Calcium By similarity UniProtKB P39116
Metal binding1801Calcium By similarity UniProtKB P39116
Metal binding1841Calcium By similarity UniProtKB P39116

Experimental info

Sequence conflict1611I → N AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
B1B6T1 [UniParc].

Last modified April 14, 2009. Version 1.
Checksum: 4662DFCBF915E9C6

FASTA34137,365
        10         20         30         40         50         60 
MKKLISIIFI FVLGVVGSLT AAVSAEAASA LNSGKVNPLA DFSLKGFAAL NGGTTGGEGG 

        70         80         90        100        110        120 
QTVTVTTGDQ LIAALKNKNA NTPLKIYVNG TITTSNTSAS KIDVKDVSNV SIVGSGTKGE 

       130        140        150        160        170        180 
LKGIGIKIWR ANNIIIRNLK IHEVASGDKD AIGIEGPSKN IWVDHNELYH SLNVDKDYYD 

       190        200        210        220        230        240 
GLFDVKRDAE YITFSWNYVH DGWKSMLMGS SDSDNYNRTI TFHHNWFENL NSRVPSFRFG 

       250        260        270        280        290        300 
EGHIYNNYFN KIIDSGINSR MGARIRIENN LFENAKDPIV SWYSSSPGYW HVSNNKFVNS 

       310        320        330        340 
RGSMPTTSTT TYNPPYSYSL DNVDNVKSIV KQNAGVGKIN P

« Hide

References

[1]"Purification, characterization, and overexpression of thermophilic pectate lyase of Bacillus sp. RN1 isolated from a hot spring in Thailand."
Sukhumsiirchart W., Kawanishi S., Deesukon W., Chansiri K., Kawasaki H., Sakamoto T.
Biosci. Biotechnol. Biochem. 73:268-273(2009) [PubMed: 19202269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-64 AND 144-161, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: RN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB428424 Genomic DNA. Translation: BAG12908.1.

3D structure databases

ProteinModelPortalB1B6T1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002022. Amb_allergen.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTSM00656. Amb_all. 1 hit.
SM00710. PbH1. 4 hits.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Entry information

Entry namePTLY_BACSP
AccessionPrimary (citable) accession number: B1B6T1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: April 14, 2009
Last modified: May 31, 2011
This is version 11 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

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