Reviewed, UniProtKB/Swiss-Prot P15698 (NANH_CLOSO)

Names and origin

Protein names	Recommended name:     Sialidase     EC=3.2.1.18 Alternative name(s):     Neuraminidase
Organism	Clostridium sordellii
Taxonomic identifier	1505 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 5 BNR repeats.

Ontologies

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	exo-alpha-sialidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Ref.1
	Chain	28 – 404	377	Sialidase		PRO_0000012030
Regions
	Repeat	89 – 100	12	BNR 1
	Repeat	158 – 169	12	BNR 2
	Repeat	226 – 237	12	BNR 3
	Repeat	273 – 284	12	BNR 4
Sites
	Active site	80	1	Proton acceptor By similarity
	Active site	365	1	Nucleophile By similarity
	Binding site	55	1	Substrate By similarity
	Binding site	263	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	P15698-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 525B9DA90083AA6A	FASTA	404	44,729
	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

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: 2693593] [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
EMBLGenBankDDBJ	M31584 Genomic DNA. Translation: AAA23280.1.
PIR	A37234.
3D structure databases
HSSP	HSSP built from PDB template 2SIL based on UniProtKB P29768.
ModBase	Search...
Protein family/group databases
CAZy	GH33. Glycoside Hydrolase Family 33.
Enzyme and pathway databases
BRENDA	3.2.1.18. 20707.
Family and domain databases
InterPro	IPR008377. Sialidase_trypan. [Graphical view]
PRINTS	PR01803. TCSIALIDASE.
PROSITE	PS51257. PROKAR_LIPOPROTEIN. 1 hit. Uncertain. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NANH_CLOSO

Accession

Primary (citable) accession number: P15698

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)