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B2FSW8 (B2FSW8_STRMK) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 18. 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 namesSubmitted name:
Putative alginate lyase protein EMBL CAQ46078.1
Gene names
Ordered Locus Names:Smlt2602
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Stenotrophomonas › Stenotrophomonas maltophilia group

Protein attributes

Sequence length742 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existencePredicted

Ontologies

Keywords
   DomainSignal EMBL CAQ46078.1
   Molecular functionLyase EMBL CAQ46078.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalginic acid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular functionpoly(beta-D-mannuronate) lyase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential EMBL CAQ46078.1
Chain32 – 742711 Potential EMBL CAQ46078.1
PRO_5000342680

Sequences

Sequence LengthMass (Da)Tools
B2FSW8 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 2E560A37F5F0A57B

FASTA74282,406
        10         20         30         40         50         60 
MRLQPLFVSL ALAAPCALLP TASLSAAPAA AARQADTAPV LVTAAQWQQM ASEGRRYPWF 

        70         80         90        100        110        120 
AKEQARTEAT LKKMMKAGID VPVPRDKGGG RTHEQHKRNY QALLAAGTLY RLTGDRAYVD 

       130        140        150        160        170        180 
YARDMLLQYA QLYPTLGPHP EGRGQIPGRV FWQVLNDSVW LVNAIQGYDA IRDALSAEDR 

       190        200        210        220        230        240 
NTIESKVFRP MAEFLVSEPK NYDQIHNHAT WAVAATGMTG YVLRDQELVE KSLRGSQKDD 

       250        260        270        280        290        300 
KFGFLRQIDL LFSPDGYYEE GPYYQRYALA PFLLFANAIE RNEPQRKIFA RRDGVLLKAV 

       310        320        330        340        350        360 
DVLVQSSYGG LFFPINDAIL DKGIDTEELV AGIGIAYART GDDRLLSVAE QQKRLLLSPE 

       370        380        390        400        410        420 
GLQVAQALAA NKAKPFDYHP MLLRDGPDGD RGGLAILRMN GERGQALVQK DTMQGMGHGH 

       430        440        450        460        470        480 
FDKLNWLFYD NGNPVVTDYG AARFLNVEAK RGGIYLAENR SWAKQTVAHN TLVVDEQSHF 

       490        500        510        520        530        540 
NGNWKRGEAH APQVRFFQAD ADTQIASATM RDAYPGVAFT RTQALLRHPD LGLPVVLDLL 

       550        560        570        580        590        600 
QVHGDKAARY DLPLHFNGHI VTTGFEAEHF PSQRPVLGKD NGYQHLWLDA RSKPGSEPRS 

       610        620        630        640        650        660 
LAWLLDGRFY TYRFGSSAPA QALLVESGAN DPEFNLRREP ALLQRVDGQK DVTFFSVLEP 

       670        680        690        700        710        720 
HGEYNGTAEY VHGADSRIRE IVRTRGSDAE VIELRLASGA RIALGVADNS ATTSEHSVTV 

       730        740 
DGHVYRWNGS HARLDRSKGD GK

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References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed: 18419807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM743169 Genomic DNA. Translation: CAQ46078.1.
RefSeqYP_001972373.1. NC_010943.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2FSW8.

Protein family/group databases

CAZyPL17. Polysaccharide Lyase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6393623.
GenomeReviewsGene locus Smlt2602 in contig AM743169_GR.
KEGGsml:Smlt2602.
PATRIC23700747. VBISteMal45202_2443.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG742331.
OMANGYQHLW.
ProtClustDBCLSK769500.

Family and domain databases

InterProIPR008397. Alginate_lyase_dom.
IPR008929. Chondroitin_lyas.
IPR012480. Hepar_II_III.
[Graphical view]
Gene3DG3DSA:1.50.10.110. Alginate_lyase. 1 hit.
PfamPF05426. Alginate_lyase. 1 hit.
PF07940. Hepar_II_III. 1 hit.
[Graphical view]
SUPFAMSSF48230. Chondroitin_lyas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB2FSW8_STRMK
AccessionPrimary (citable) accession number: B2FSW8
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: December 14, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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