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P26831 (NAGH_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronoglucosaminidase
Short name=Hyaluronidase
EC=3.2.1.35
Alternative name(s):
Mu toxin
Gene names
Name:nagH
Ordered Locus Names:CPE0191
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length1628 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative virulence factor which is likely to act on connective tissue during gas gangrene.

Catalytic activity

Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

Subcellular location

Secreted.

Sequence similarities

Contains 1 F5/8 type C domain.

Caution

The partially purified protein from strain CPN50 is approximately 70 kDa smaller than the sequence indicated here.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Toxin
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: InterPro

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhyalurononglucosaminidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 16281598Hyaluronoglucosaminidase
PRO_0000021787

Regions

Domain781 – 953173F5/8 type C

Natural variations

Natural variant1471G → A in strain: CPN50.
Natural variant172 – 1754KIQS → EIKN in strain: CPN50.
Natural variant2501V → M in strain: CPN50.
Natural variant5481A → E in strain: CPN50.
Natural variant5581D → E in strain: CPN50.
Natural variant6141G → S in strain: CPN50.
Natural variant9441I → V in strain: CPN50.
Natural variant9501N → S in strain: CPN50.
Natural variant9791T → I in strain: CPN50.
Natural variant9821I → L in strain: CPN50.
Natural variant10421I → F in strain: CPN50.
Natural variant1043 – 1628586Missing in strain: CPN50.

Secondary structure

1 ............................................... 1628
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26831 [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: D4252A2512BBED69

FASTA1,628182,475
        10         20         30         40         50         60 
MNKNIRKIIT STVLAAMTIS VLPSNLVVFA TDGITENFYE IYPKPQEISY SGGEFQISDE 

        70         80         90        100        110        120 
INIVYDDGID TYTKKRVDEV LEASNLEATV SNEIVPGKTN FLVGINESGG VVDNYFNKNI 

       130        140        150        160        170        180 
PHDESFFDEK MDANIVSVKD GVIGVIGEDT DSAFYGVTTL KHVFNQLEEG NKIQSFRADD 

       190        200        210        220        230        240 
YAEVAHRGFI EGYYGNPWSN EDRAELMKFG GDYKLNQYVF APKDDPYHNS KWRDLYPEEK 

       250        260        270        280        290        300 
LSEIKKLAQV GNETKNRYVY ALHPFMNNPV RFDTEENYQN DLGVIKAKFT QLLENDVRQF 

       310        320        330        340        350        360 
AILADDASAP AQGASMYVKL LTDLTRWLEE QQSTYPDLKT DLMFCPSDYY GNGSSAQLKE 

       370        380        390        400        410        420 
LNKAEDNVSI VMTGGRIWGE VDENFANNFM NNISTEGHPG RAPFFWINWP CSDNSKQHLI 

       430        440        450        460        470        480 
MGGNDTFLHP GVDPSKIDGI VLNPMQQAEA NKSALFAIAD YAWNIWDNKE EADENWNDSF 

       490        500        510        520        530        540 
KYMDHGTAEE TNSSLALREI SKHMINQNMD GRVRPLQESV ELAPKLEAFK QKYDSGASIK 

       550        560        570        580        590        600 
EDALELIAEF TNLQKAADYY KNNPGNERTR DQIIYWLNCW EDTMDAAIGY LKSAIAIEEG 

       610        620        630        640        650        660 
DDEAAWANYS EAQGAFEKSK TYGFHYVDHT EYAEVGVQHI VPFIKSMGQN LSVVIGSIVD 

       670        680        690        700        710        720 
PNRIIATYIS NRQDAPTGNP DNIFDNNAST ELVYKNPNRI DVGTYVGVKY SNPITLNNVE 

       730        740        750        760        770        780 
FLMGANSNPN DTMQKAKIQY TVDGREWIDL EEGVEYTMPG AIKVENLDLK VRGVRLIATE 

       790        800        810        820        830        840 
ARENTWLGVR DINVNKKEDS NSGVEFNPSL IRSESWQVYE GNEANLLDGD DNTGVWYKTL 

       850        860        870        880        890        900 
NGDTSLAGEF IGLDLGKEIK LDGIRFVIGK NGGGSSDKWN KFKLEYSLDN ESWTTIKEYD 

       910        920        930        940        950        960 
KTGAPAGKDV IEESFETPIS AKYIRLTNME NINKWLTFSE FAIISDELEN AGNKENVYTN 

       970        980        990       1000       1010       1020 
TELDLLSLAK EDVTKLIPTD DISLNHGEYI GVKLNRIKDL SNINLEISND TGLKLQSSMN 

      1030       1040       1050       1060       1070       1080 
GVEWTEITDK NTLEDGRYVR LINTSNEAVN FNLTKFEVNS NEVYEPSLVD AYVGDDGAKK 

      1090       1100       1110       1120       1130       1140 
AVDGDLKTRV KFLGAPSTGD TIVYDLGQEI LVDNLKYVVL DTEVDHVRDG KIQLSLDGET 

      1150       1160       1170       1180       1190       1200 
WTDAITIGDG VENGVDDMFS TPLKNGYKHG NQSGGIVPID SAYVEGDNLN QKARYVRILF 

      1210       1220       1230       1240       1250       1260 
TAPYRHRWTV INELMINNGE YISTVNDPTY ISNPIEERGF APSNLRDGNL TTSYKPNTNN 

      1270       1280       1290       1300       1310       1320 
GEISEGSITY RLSEKTDVRK VTIVQSGSSI SNAKVMARVG DGSENVTDQW VQLGTLSNSL 

      1330       1340       1350       1360       1370       1380 
NEFINRDYNN IYEIKIEWTD VAPNIYEIIT LNQEFEFPVN DSLKAKYDEL INLSGDEYTL 

      1390       1400       1410       1420       1430       1440 
SSFETLKEAL NEAKSILDDS NSSQKKIDKA LEKLNKAEER LDLRATDFED FNKVLTLGNS 

      1450       1460       1470       1480       1490       1500 
LVEEEYTAES WALFSEVLEA ANEANKNKAD YTQDQINQIV IDLDASIKAL VKETPEVDKT 

      1510       1520       1530       1540       1550       1560 
NLGELINQGK SLLDESVEGF NVGEYHKGAK DGLTVEINKA EEVFNKEDAT EEEINLAKES 

      1570       1580       1590       1600       1610       1620 
LEGAIARFNS LLIEESTGDF NGNGKIDIGD LAMVSKNIGS TTNTSLDLNK DGSIDEYEIS 


FINHRILN

« Hide

References

« Hide 'large scale' references
[1]"Molecular genetic analysis of the nagH gene encoding a hyaluronidase of Clostridium perfringens."
Canard B., Garnier T., Saint-Joanis B., Cole S.T.
Mol. Gen. Genet. 243:215-224(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CPN50.
[2]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M81878 Genomic DNA. Translation: AAA23259.1.
BA000016 Genomic DNA. Translation: BAB79897.1.
PIRS43904.
RefSeqNP_561107.1. NC_003366.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JNKNMR-A1498-1628[»]
2OZNX-ray1.60B1498-1628[»]
2W1QX-ray1.60A/B807-975[»]
2W1SX-ray1.45A/B807-975[»]
2W1UX-ray2.00A/B/C/D807-975[»]
2WDBX-ray2.03A/B/C/D807-975[»]
ProteinModelPortalP26831.
SMRP26831. Positions 1498-1628.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46268N.
STRING195102.CPE0191.

Protein family/group databases

CAZyCBM32. Carbohydrate-Binding Module Family 32.
GH84. Glycoside Hydrolase Family 84.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB79897; BAB79897; BAB79897.
GeneID988432.
KEGGcpe:CPE0191.
PATRIC19494262. VBICloPer59675_0248.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG69445.
HOGENOMHOG000113726.
KOK01197.
OMAHTEYAEV.
ProtClustDBCLSK518480.

Enzyme and pathway databases

BioCycCPER195102:GJFM-216-MONOMER.
BRENDA4.2.2.1. 1503.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
InterProIPR011496. Beta-N-acetylglucosaminidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR011490. Extracell_matric-bd_Ebh.
IPR008979. Galactose-bd-like.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00754. F5_F8_type_C. 2 hits.
PF07554. FIVAR. 3 hits.
PF07555. NAGidase. 1 hit.
[Graphical view]
SMARTSM00231. FA58C. 1 hit.
[Graphical view]
SUPFAMSSF63446. Cellulos_enz_dockerin_1. 1 hit.
SSF49785. Gal_bind_like. 4 hits.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS50022. FA58C_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26831.

Entry information

Entry nameNAGH_CLOPE
AccessionPrimary (citable) accession number: P26831
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 31, 2002
Last modified: May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents