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P15698 (NANH_CLOSO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialidase

EC=3.2.1.18
Alternative name(s):
Neuraminidase
OrganismClostridium sordellii
Taxonomic identifier1505 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceae

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sialidases have been suggested to be pathogenic factors in microbial infections.

Catalytic activity

Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

Subcellular location

Secreted.

Post-translational modification

It is possible that the sialidase is cleaved in front of a cysteine within the leader peptide, forming a glyceride thioether bond which links the protein to the membrane. A second proteolytic cleavage releases the mature extracellular protein.

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 4 BNR repeats.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionexo-alpha-(2->3)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->6)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->8)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 404377Sialidase
PRO_0000012030

Regions

Repeat89 – 10012BNR 1
Repeat158 – 16912BNR 2
Repeat226 – 23712BNR 3
Repeat273 – 28412BNR 4

Sites

Active site801Proton acceptor By similarity
Active site3651Nucleophile By similarity
Binding site551Substrate By similarity
Binding site2631Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
P15698 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 525B9DA90083AA6A

FASTA40444,729
        10         20         30         40         50         60 
MKKFIKILKV LSMAIVLSAC NINGIFASNL NTTNEPQKTT VFNKNDNTWN AQYFRIPSLQ 

        70         80         90        100        110        120 
TLADGTMLAF SDIRYNGAED HAYIDIGAAK STDNGQTWDY KTVMENDRID STFSRVMDST 

       130        140        150        160        170        180 
TVVTDTGRII LIAGSWNKNG NWASSTTSLR SDWSVQMVYS DDNGETWSDK VDLTTNKARI 

       190        200        210        220        230        240 
KNQPSNTIGW LAGVGSGIVM SDGTIVMPIQ IALRENNANN YYSSVIYSKD NGETWTMGNK 

       250        260        270        280        290        300 
VPDPKTSENM VIELDGALIM SSRNDGKNYR ASYISYDMGS TWEVYDPLHN KISTGNGSGC 

       310        320        330        340        350        360 
QGSFIKVTAK DGHRLGFISA PKNTKGGYVR DNITVYMIDF DDLSKGIREL CSPYPEDGNS 

       370        380        390        400 
SGGGYSCLSF NDGKLSILYE ANGNIEYKDL TDYYLSIENN KKLK 

« Hide

References

[1]"Cloning, sequencing and expression of a sialidase gene from Clostridium sordellii G12."
Rothe B., Roggentin P., Frank R., Bloecker H., Schauer R.
J. Gen. Microbiol. 135:3087-3096(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-45.
Strain: ATCC 9714 / DSM 2141 / JCM 3814 / LMG 15708 / NCIB 10717.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31584 Genomic DNA. Translation: AAA23280.1.
PIRA37234.

3D structure databases

ProteinModelPortalP15698.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR002860. BNR_rpt.
IPR026948. Sialidase/anhydrosialidase.
IPR026856. Sialidase_fam.
IPR008377. Sialidase_trypan.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF5. PTHR10628:SF5. 1 hit.
PfamPF02012. BNR. 3 hits.
[Graphical view]
PRINTSPR01803. TCSIALIDASE.
SUPFAMSSF50939. SSF50939. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNANH_CLOSO
AccessionPrimary (citable) accession number: P15698
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 19, 2014
This is version 85 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries