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Reviewed, UniProtKB/Swiss-Prot O34310 (PELC_BACSU)

Last modified November 25, 2008. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Pectate lyase
    EC=4.2.2.2
Gene names
Name: pelC
Synonyms: yvpA
Ordered Locus Names: BSU34950
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in depolymerization of polygalacturonate and pectins with different degree of methyl esterification. Cleaves bonds by beta-elimination. In contrast to known pectate lyases, it shows high activity on highly methylated pectins.

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-gluconic acid from pectin: step 2/5.

Subcellular location

Secreted.

Miscellaneous

Hg(2+) could replace calcium ion.

Sequence similarities

Belongs to the polysaccharide lyase 3 family.

Biophysicochemical properties

Kinetic parameters:

Vmax=256.7 µmol/min/mg enzyme toward 22% esterified pectin

Vmax=59.6 µmol/min/mg enzyme toward polygalacturonic acid

pH dependence:

Optimum pH is 10.

Temperature dependence:

Optimum temperature is 65 degrees Celsius. Thermostable at 50 degrees Celsius in buffers at pH 7.

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Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome

Gene Ontology (GO)

   Cellular componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 221194Pectate lyase
PRO_0000233104

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Sequences

Sequence LengthMass (Da)Tools
O34310-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: AB324700DE573236

FASTA22124,281
        10         20         30         40         50         60 
MKKIVSILFM FGLVMGFSQF QPSTVFAADK VVHETIIVPK NTTYDGKGQR FVAGKELGDG 

        70         80         90        100        110        120 
SQSENQDPVF RVEDGATLKN VVLGAPAADG VHTYGNVNIQ NVKWEDVGED ALTVKKEGKV 

       130        140        150        160        170        180 
TIDGGSAQKA SDKIFQINKA STFTVKNFTA DNGGKFIRQL GGSTFHVDVI IDKCTITNMK 

       190        200        210        220 
EAIFRTDSKT STVRMTNTRY SNVGQKWIGV QHIYENNNTQ F

« Hide

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References

« Hide 'large scale' references
[1]"Nucleotide sequence of the 300-304 chromosomal segment of Bacillus subtilis."
Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin."
Soriano M., Diaz P., Pastor F.I.J.
Microbiology 152:617-625(2006) [PubMed: 16514142] [Abstract]
Cited for: CHARACTERIZATION.
Strain: 168.

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Cross-references

Sequence databases

AF017113 Genomic DNA. Translation: AAC67291.1.
Z99121 Genomic DNA. Translation: CAB15500.1.
PIRA70045.
RefSeqNP_391375.1.

3D structure databases

HSSPHSSP built from PDB template 1EE6 based on UniProtKB Q9RHW0.
ModBaseSearch...

Genome annotation databases

GeneID936594.
GenomeReviewsGene locus BSU34950 in contig AL009126_GR.
KEGGbsu:BSU34950.
NMPDRfig|224308.1.peg.3501.

Organism-specific databases

SubtiListBG14129. yvpA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO34310.

Enzyme and pathway databases

BioCycBSUB224308:BSU3492-MON.

Family and domain databases

InterProIPR004898. Pectate_lyase_cat.
IPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF03211. Pectate_lyase. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePELC_BACSU
AccessionPrimary (citable) accession number: O34310
Secondary accession number(s): Q795F2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: January 1, 1998
Last modified: November 25, 2008
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents