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P15698

- NANH_CLOSO

UniProt

P15698 - NANH_CLOSO

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Protein

Sialidase

Gene
N/A
Organism
Clostridium sordellii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551SubstrateBy similarity
Active sitei80 – 801Proton acceptorBy similarity
Binding sitei263 – 2631SubstrateSequence Analysis
Active sitei365 – 3651NucleophileBy similarity

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC

GO - Biological processi

  1. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Sialidase (EC:3.2.1.18)
Alternative name(s):
Neuraminidase
OrganismiClostridium sordellii
Taxonomic identifieri1505 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationPROSITE-ProRule annotationAdd
BLAST
Chaini28 – 404377SialidasePRO_0000012030Add
BLAST

Post-translational modificationi

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.

Structurei

3D structure databases

ProteinModelPortaliP15698.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati89 – 10012BNR 1Add
BLAST
Repeati158 – 16912BNR 2Add
BLAST
Repeati226 – 23712BNR 3Add
BLAST
Repeati273 – 28412BNR 4Add
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 33 family.Curated
Contains 4 BNR repeats.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR002860. BNR_rpt.
IPR026856. Sialidase_fam.
IPR008377. Sialidase_trypan.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF5. PTHR10628:SF5. 1 hit.
PfamiPF02012. BNR. 3 hits.
[Graphical view]
PRINTSiPR01803. TCSIALIDASE.
SUPFAMiSSF50939. SSF50939. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15698-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKFIKILKV LSMAIVLSAC NINGIFASNL NTTNEPQKTT VFNKNDNTWN
60 70 80 90 100
AQYFRIPSLQ TLADGTMLAF SDIRYNGAED HAYIDIGAAK STDNGQTWDY
110 120 130 140 150
KTVMENDRID STFSRVMDST TVVTDTGRII LIAGSWNKNG NWASSTTSLR
160 170 180 190 200
SDWSVQMVYS DDNGETWSDK VDLTTNKARI KNQPSNTIGW LAGVGSGIVM
210 220 230 240 250
SDGTIVMPIQ IALRENNANN YYSSVIYSKD NGETWTMGNK VPDPKTSENM
260 270 280 290 300
VIELDGALIM SSRNDGKNYR ASYISYDMGS TWEVYDPLHN KISTGNGSGC
310 320 330 340 350
QGSFIKVTAK DGHRLGFISA PKNTKGGYVR DNITVYMIDF DDLSKGIREL
360 370 380 390 400
CSPYPEDGNS SGGGYSCLSF NDGKLSILYE ANGNIEYKDL TDYYLSIENN

KKLK
Length:404
Mass (Da):44,729
Last modified:April 1, 1990 - v1
Checksum:i525B9DA90083AA6A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31584 Genomic DNA. Translation: AAA23280.1.
PIRiA37234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31584 Genomic DNA. Translation: AAA23280.1 .
PIRi A37234.

3D structure databases

ProteinModelPortali P15698.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR002860. BNR_rpt.
IPR026856. Sialidase_fam.
IPR008377. Sialidase_trypan.
IPR011040. Sialidases.
[Graphical view ]
PANTHERi PTHR10628. PTHR10628. 1 hit.
PTHR10628:SF5. PTHR10628:SF5. 1 hit.
Pfami PF02012. BNR. 3 hits.
[Graphical view ]
PRINTSi PR01803. TCSIALIDASE.
SUPFAMi SSF50939. SSF50939. 1 hit.
PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiNANH_CLOSO
AccessioniPrimary (citable) accession number: P15698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3