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Reviewed, UniProtKB/Swiss-Prot Q53591 (HYSA_STRA3)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Hyaluronate lyase
    EC=4.2.2.1
Alternative name(s):
    Hyaluronidase
      Short name=HYase
Gene names
Name: hylB
Ordered Locus Names: gbs1270
OrganismStreptococcus agalactiae serotype III [Complete proteome] [HAMAP]
Taxonomic identifier216495 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

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Protein attributes

Sequence length984 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.

Subcellular location

Secreted.

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

hyaluronate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 Potential
Chain41 – 984944Hyaluronate lyase
PRO_0000024932

Sites

Active site4291
Active site4791
Active site4881

Experimental info

Sequence conflict451E → G in AAA56749. Ref.1
Sequence conflict155 – 1562SA → FV in AAA56749. Ref.1
Sequence conflict1831E → K in AAA56749. Ref.1
Sequence conflict246 – 2516ASTEDK → GSPEDN in AAA56749. Ref.1
Sequence conflict2671H → Y in AAA56749. Ref.1
Sequence conflict279 – 2802IN → LT in AAA56749. Ref.1
Sequence conflict2881A → G in AAA56749. Ref.1
Sequence conflict292 – 2932KT → EA in AAA56749. Ref.1
Sequence conflict3001H → R in AAA56749. Ref.1
Sequence conflict3841A → G in AAA56749. Ref.1
Sequence conflict3871A → S in AAA56749. Ref.1
Sequence conflict4131G → E in AAA56749. Ref.1
Sequence conflict4201D → V in AAA56749. Ref.1
Sequence conflict5831T → A in AAA56749. Ref.1
Sequence conflict6091M → L in AAA56749. Ref.1
Sequence conflict6391E → K in AAA56749. Ref.1
Sequence conflict6661D → G in AAA56749. Ref.1
Sequence conflict6761L → I in AAA56749. Ref.1
Sequence conflict688 – 6892FW → LG in AAA56749. Ref.1
Sequence conflict8821Q → L in AAA56749. Ref.1
Sequence conflict8941M → L in AAA56749. Ref.1

Secondary structure

1 ................................................................................................................................. 984
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q53591-1 [UniParc].

Last modified January 17, 2003. Version 2.
Checksum: AC7215ED6D5C2592

FASTA984111,581
        10         20         30         40         50         60 
MKQVVDNQTQ NKELVKNGDF NQTNPVSGSW SHTSAREWSA WIDKENTADK SPIIQRTEQG 

        70         80         90        100        110        120 
QVSLSSDKGF RGAVTQKVNI DPTKKYEVKF DIETSNKAGQ AFLRIMEKKD NNTRLWLSEM 

       130        140        150        160        170        180 
TSGTTNKHTL TKIYNPKLNV SEVTLELYYE KGTGSATFDN ISMKAKGPKD SEHPQPVTTQ 

       190        200        210        220        230        240 
IEESVNTALN KNYVFNKADY QYTLTNPSLG KIVGGILYPN ATGSTTVKIS DKSGKIIKEV 

       250        260        270        280        290        300 
PLSVTASTED KFTKLLDKWN DVTIGNHVYD TNDSNMQKIN QKLDETNAKN IKTIKLDSNH 

       310        320        330        340        350        360 
TFLWKDLDNL NNSAQLTATY RRLEDLAKQI TNPHSTIYKN EKAIRTVKES LAWLHQNFYN 

       370        380        390        400        410        420 
VNKDIEGSAN WWDFEIGVPR SITATLALMN NYFTDAEIKT YTDPIEHFVP DAGYFRKTLD 

       430        440        450        460        470        480 
NPFKALGGNL VDMGRVKIIE GLLRKDNTII EKTSHSLKNL FTTATKAEGF YADGSYIDHT 

       490        500        510        520        530        540 
NVAYTGAYGN VLIDGLTQLL PIIQETDYKI SNQELDMVYK WINQSFLPLI VKGELMDMSR 

       550        560        570        580        590        600 
GRSISREAAS SHAAAVEVLR GFLRLANMSN EERNLDLKST IKTIITSNKF YNVFNNLKSY 

       610        620        630        640        650        660 
SDIANMNKML NDSTVATKPL KSNLSTFNSM DRLAYYNAEK DFGFALSLHS KRTLNYEGMN 

       670        680        690        700        710        720 
DENTRDWYTG DGMFYLYNSD QSHYSNHFWP TVNPYKMAGT TEKDAKREDT TKEFMSKHSK 

       730        740        750        760        770        780 
DAKEKTGQVT GTSDFVGSVK LNDHFALAAM DFTNWDRTLT AQKGWVILND KIVFLGSNIK 

       790        800        810        820        830        840 
NTNGIGNVST TIDQRKDDSK TPYTTYVNGK TIDLKQASSQ QFTDTKSVFL ESKEPGRNIG 

       850        860        870        880        890        900 
YIFFKNSTID IERKEQTGTW NSINRTSKNT SIVSNPFITI SQKHDNKGDS YGYMMVPNID 

       910        920        930        940        950        960 
RTSFDKLANS KEVELLENSS KQQVIYDKNS QTWAVIKHDN QESLINNQFK MNKAGLYLVQ 

       970        980 
KVGNDYQNVY YQPQTMTKTD QLAI

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References

« Hide 'large scale' references
[1]"Cloning and expression of the gene for group B streptococcal hyaluronate lyase."
Lin B., Hollingshead S.K., Coligan J.E., Egan M.L., Baker J.R., Pritchard D.G.
J. Biol. Chem. 269:30113-30116(1994) [PubMed: 7982914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 3502 / Serotype III.
[2]"Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease."
Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.
Mol. Microbiol. 45:1499-1513(2002) [PubMed: 12354221] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NEM316 / Serotype III.
[3]"Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase."
Li S., Jedrzejas M.J.
J. Biol. Chem. 276:41407-41416(2001) [PubMed: 11527972] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 171-984.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U15050 Genomic DNA. Translation: AAA56749.1.
AL766849 Genomic DNA. Translation: CAD46929.1. Different initiation.
PIRA55137.
RefSeqNP_735714.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1F1SX-ray2.10A171-984[»]
1I8QX-ray2.20A171-984[»]
1LXMX-ray2.20A171-984[»]
ModBaseSearch...

Protein family/group databases

CAZyPL8. Polysaccharide Lyase Family 8.

Genome annotation databases

GeneID1030294.
GenomeReviewsGene locus gbs1270 in contig AL732656_GR.
KEGGsan:gbs1270.

Organism-specific databases

SagaListgbs1270.
CMRSearch...

Phylogenomic databases

HOGENOMQ53591.

Enzyme and pathway databases

BioCycSAGA211110:GBS1270-MON.
BRENDA4.2.2.1. 3065.

Family and domain databases

InterProIPR014718. Glyco_hydro-type_carb-bd_sub.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central.
IPR012329. Lyase_8_N.
[Graphical view]
Gene3DG3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit.
G3DSA:1.50.10.100. Lyase_8_N. 1 hit.
PfamPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHYSA_STRA3
AccessionPrimary (citable) accession number: Q53591
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 17, 2003
Last modified: June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents