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A1JSS8 (A1JSS8_YERE8) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 28. Feed History...

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

Protein names
Gene names
Name:pelY EMBL CAL14085.1
Ordered Locus Names:YE4069
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

Ontologies

Keywords
   DomainSignal EMBL CAL14085.1
   Molecular functionLyase EMBL CAL14085.1
   Technical term3D-structure PDB 2V8I PDB 2V8K PDB 2V8J
Complete proteome
Gene Ontology (GO)
   Biological processpectin catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbon-oxygen lyase activity, acting on polysaccharides

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential EMBL CAL14085.1
Chain24 – 572549 Potential EMBL CAL14085.1
PRO_5000201446

Sites

Metal binding1321Manganese; via tele nitrogen PDB 2V8J
Metal binding1531Manganese PDB 2V8J
Metal binding1951Manganese; via tele nitrogen PDB 2V8J

Sequences

Sequence LengthMass (Da)Tools
A1JSS8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 97570E4461B0BE98

FASTA57264,263
        10         20         30         40         50         60 
MKKRALFLSM AALATLYIPA GQAADTDRLT VVKQYVDNVL NKASDTYHGD KPSPLLADGV 

        70         80         90        100        110        120 
DPRTGQQLEW IFPDGRRAVL SNFSAQQNLM RVMSGLSQLS GDPRYQKRAE DIVRYHFQNY 

       130        140        150        160        170        180 
QDPSGLLYWG GHRFVDLKTL QPEGPSEKEM VHELKNAYPY YDLMFSVDSD ATARFIRGFW 

       190        200        210        220        230        240 
NAHVYDWRIL ETSRHGEYGK PMGALWESKF EQQPPFFATK GLSFLNAGND LIYSASLLYK 

       250        260        270        280        290        300 
HQQDQGALTW AKRLADQYVL PRDAKTGLGV YQFTQALKRE EPTDDADTHS KFGDRAQRQF 

       310        320        330        340        350        360 
GPEFGPTALE GNMMLKGRTS TLYSENALMQ LQLGKDLGPQ GQDLLKWTVD GLKAFAKYAY 

       370        380        390        400        410        420 
NDQDNTFRPM IANGQDLSNY TLPRDGYYGK KGTVLKPYKA GNEFLISYAR AYAIDNDPLL 

       430        440        450        460        470        480 
WKVARGIAND QGLGDIGTAP GKEVKVNMDT TNSDPYALFA LLDLYHASQV ADYRKLAEKI 

       490        500        510        520        530        540 
GDNIIKIRYI DGFFMASSDR QYADVDAIEP YALLALEASL RNKPQAVAPF LNGAGFTEGA 

       550        560        570 
YRMDDGSARV STRDNELFLL NVGEKLQPNG RK 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed: 17173484] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"A family 2 pectate lyase displays a rare fold and transition metal-assisted beta-elimination."
Abbott D.W., Boraston A.B.
J. Biol. Chem. 282:35328-35336(2007) [PubMed: 17881361] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-569.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL14085.1.
RefSeqYP_001008209.1. NC_008800.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V8IX-ray1.50A27-569[»]
2V8JX-ray2.01A28-562[»]
2V8KX-ray2.10A27-569[»]
ProteinModelPortalA1JSS8.
SMRA1JSS8. Positions 27-569.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1JSS8.

Protein family/group databases

CAZyPL2. Polysaccharide Lyase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4716358.
GenomeReviewsGene locus YE4069 in contig AM286415_GR.
KEGGyen:YE4069.
NMPDRfig|630.2.peg.3995.
PATRIC18568006. VBIYerEnt11519_4328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG41513.
HOGENOMHBG472751.
OMARPMLANG.
ProtClustDBCLSK888942.

Enzyme and pathway databases

BioCycYENT393305:YE4069-MONOMER.

Family and domain databases

InterProIPR010702. Pectate_lyase_2.
[Graphical view]
KOK01728.
PfamPF06917. Pectate_lyase_2. 1 hit.
[Graphical view]
PIRSFPIRSF001432. Pect_lyase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA1JSS8_YERE8
AccessionPrimary (citable) accession number: A1JSS8
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)