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Reviewed, UniProtKB/Swiss-Prot Q54873 (HYSA_STRPN)

Last modified June 15, 2010. Version 94. 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 originHide

Protein namesRecommended name:
Hyaluronate lyase
EC=4.2.2.1
Alternative name(s):
Hyaluronidase
Short name=HYase
Gene names
Ordered Locus Names:SP_0314
OrganismStreptococcus pneumoniae [Complete proteome] [HAMAP]
Taxonomic identifier1313 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus
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Protein attributesHide

Sequence length1066 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)Hide

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 › cell wall; Peptidoglycan-anchor Potential.

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

Sequence caution

The sequence AAA53685.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA53686.1 differs from that shown. Reason: Erroneous initiation.

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OntologiesHide

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionLyase
   PTMPeptidoglycan-anchor
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   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)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 10391009Hyaluronate lyase
PRO_0000024933
Propeptide1040 – 106627Removed by sortase Potential
PRO_0000024934

Regions

Motif1036 – 10405LPXTG sorting signal Potential

Sites

Active site4661
Active site5161
Active site5251

Amino acid modifications

Modified residue10391Pentaglycyl murein peptidoglycan amidated threonine Potential

Experimental info

Mutagenesis3601R → V: Retains 67% of wild-type activity. Ref.4
Mutagenesis4661N → A: Almost complete loss of activity. Ref.4
Mutagenesis5161H → A: Almost complete loss of activity. Ref.4
Mutagenesis5251Y → F: Complete loss of activity. Ref.4
Mutagenesis6971N → G: Slightly increased activity. Ref.4
Sequence conflict1081H → P Ref.2
Sequence conflict1151L → V Ref.2
Sequence conflict1391I → V in AAA53685. Ref.2
Sequence conflict2111L → P in AAA53685. Ref.2
Sequence conflict2361S → P in AAA53685. Ref.2
Sequence conflict2901A → T in AAA53685. Ref.2
Sequence conflict2901A → T in AAA53686. Ref.2
Sequence conflict3131E → D in AAA53685. Ref.2
Sequence conflict3131E → D in AAA53686. Ref.2
Sequence conflict3401T → I in AAA53685. Ref.2
Sequence conflict3401T → I in AAA53686. Ref.2
Sequence conflict6131C → R in AAA53685. Ref.2
Sequence conflict6131C → R in AAA53686. Ref.2
Sequence conflict6581P → T in AAA53685. Ref.2
Sequence conflict6581P → T in AAA53686. Ref.2
Sequence conflict8211G → S in AAA53685. Ref.2
Sequence conflict8211G → S in AAA53686. Ref.2
Sequence conflict8481V → G in AAA53685. Ref.2
Sequence conflict8481V → G in AAA53686. Ref.2
Sequence conflict8531F → S in AAA53685. Ref.2
Sequence conflict8531F → S in AAA53686. Ref.2
Sequence conflict9071R → G in AAA53685. Ref.2
Sequence conflict9071R → G in AAA53686. Ref.2

Secondary structure

1 ............................................................................................................................. 1066
Helix Strand Turn

Details...

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SequencesHide

Sequence LengthMass (Da)Tools
Q54873-1 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 81DB22A837BE61F9

FASTA1,066120,771
        10         20         30         40         50         60 
MQTKTKKLIV SLSSLVLSGF LLNHYMTIGA EETTTNTIQQ SQKEVQYQQR DTKNLVENGD 

        70         80         90        100        110        120 
FGQTEDGSSP WTGSKAQGWS AWVDQKNSAD ASTRVIEAKD GAITISSHEK LRAALHRMVP 

       130        140        150        160        170        180 
IEAKKKYKLR FKIKTDNKIG IAKVRIIEES GKDKRLWNSA TTSGTKDWQT IEADYSPTLD 

       190        200        210        220        230        240 
VDKIKLELFY ETGTGTVSFK DIELVEVADQ LSEDSQTDKQ LEEKIDLPIG KKHVFSLADY 

       250        260        270        280        290        300 
TYKVENPDVA SVKNGILEPL KEGTTNVIVS KDGKEVKKIP LKILASVKDA YTDRLDDWNG 

       310        320        330        340        350        360 
IIAGNQYYDS KNEQMAKLNQ ELEGKVADSL SSISSQADRT YLWEKFSNYK TSANLTATYR 

       370        380        390        400        410        420 
KLEEMAKQVT NPSSRYYQDE TVVRTVRDSM EWMHKHVYNS EKSIVGNWWD YEIGTPRAIN 

       430        440        450        460        470        480 
NTLSLMKEYF SDEEIKKYTD VIEKFVPDPE HFRKTTDNPF KALGGNLVDM GRVKVIAGLL 

       490        500        510        520        530        540 
RKDDQEISST IRSIEQVFKL VDQGEGFYQD GSYIDHTNVA YTGAYGNVLI DGLSQLLPVI 

       550        560        570        580        590        600 
QKTKNPIDKD KMQTMYHWID KSFAPLLVNG ELMDMSRGRS ISRANSEGHV AAVEVLRGIH 

       610        620        630        640        650        660 
RIADMSEGET KQCLQSLVKT IVQSDSYYDV FKNLKTYKDI SLMQSLLSDA GVASVPRPSY 

       670        680        690        700        710        720 
LSAFNKMDKT AMYNAEKGFG FGLSLFSSRT LNYEHMNKEN KRGWYTSDGM FYLYNGDLSH 

       730        740        750        760        770        780 
YSDGYWPTVN PYKMPGTTET DAKRADSDTG KVLPSAFVGT SKLDDANATA TMDFTNWNQT 

       790        800        810        820        830        840 
LTAHKSWFML KDKIAFLGSN IQNTSTDTAA TTIDQRKLES GNPYKVYVND KEASLTEQEK 

       850        860        870        880        890        900 
DYPETQSVFL ESFDSKKNIG YFFFKKSSIS MSKALQKGAW KDINEGQSDK EVENEFLTIS 

       910        920        930        940        950        960 
QAHKQNRDSY GYMLIPNVDR ATFNQMIKEL ESSLIENNET LQSVYDAKQG VWGIVKYDDS 

       970        980        990       1000       1010       1020 
VSTISNQFQV LKRGVYTIRK EGDEYKIAYY NPETQESAPD QEVFKKLEQA AQPQVQNSKE 

      1030       1040       1050       1060 
KEKSEEEKNH SDQKNLPQTG EGQSILASLG FLLLGAFYLF RRGKNN

« Hide

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ReferencesHide

« Hide 'large scale' references
[1]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed: 11463916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
[2]"Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli."
Berry A.M., Lock R.A., Thomas S.M., Rajan D.P., Hansman D., Paton J.C.
Infect. Immun. 62:1101-1108(1994) [PubMed: 8112843] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-1066.
Strain: Type 23.
[3]"Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase."
Jedrzejas M.J., Chantalat L., Mewbourne R.B.
J. Struct. Biol. 121:73-75(1998) [PubMed: 9573623] [Abstract]
Cited for: CRYSTALLIZATION.
[4]"Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase."
Li S., Kelly S.J., Lamani E., Ferraroni M., Jedrzejas M.J.
EMBO J. 19:1228-1240(2000) [PubMed: 10716923] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 285-1015, MUTAGENESIS OF ARG-360; ASN-466; HIS-516; TYR-525 AND ASN-697.
+Additional computationally mapped references.
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ		AE005672 Genomic DNA. Translation: AAK74491.1.
L20670 Genomic DNA. Translation: AAA53685.1. Different initiation.
L20670 Genomic DNA. Translation: AAA53686.1. Different initiation.
PIRB95037.
RefSeqNP_344851.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C82X-ray1.70A285-1009[»]
1EGUX-ray1.56A285-1009[»]
1F9GX-ray2.00A285-1009[»]
1LOHX-ray2.00A287-1007[»]
1LXKX-ray1.53A287-1007[»]
1N7NX-ray1.55A287-1007[»]
1N7OX-ray1.50A287-1007[»]
1N7PX-ray1.55A287-1007[»]
1N7QX-ray2.30A287-1007[»]
1N7RX-ray2.20A287-1007[»]
1OJMX-ray1.78A287-1009[»]
1OJNX-ray1.60A285-1009[»]
1OJOX-ray1.75A285-1009[»]
1OJPX-ray1.90A285-1009[»]
1W3YX-ray1.65A297-1009[»]
2BRPX-ray2.00A285-1009[»]
2BRVX-ray3.30X285-1009[»]
2BRWX-ray2.80A/B285-1009[»]
SMRQ54873. Positions 212-1001.
ModBaseSearch...

Protein family/group databases

CAZyPL8. Polysaccharide Lyase Family 8.

Genome annotation databases

EnsemblBacteriaEBSTRT00000025915; EBSTRP00000025007; EBSTRG00000025915.
GeneID930127.
GenomeReviewsGene locus SP_0314 in contig AE005672_GR.
KEGGspn:SP_0314.
TIGRSP_0314.

Phylogenomic databases

HOGENOMHBG698564.
OMATTIDQRK.
ProtClustDBCLSK559792.

Enzyme and pathway databases

BRENDA4.2.2.1. 600.

Family and domain databases

InterProIPR008929. Chondroitin_lyas.
IPR008979. Galactose-bd-like.
IPR011013. Glyco_hydro-type_carb-bd.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR014756. Ig_E-set.
IPR019931. LPXTG-motif_cell_wall_anchor.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
[Graphical view]
Gene3DG3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit.
G3DSA:2.60.220.10. Lyase_8_C. 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]
SUPFAMSSF48230. Chondroitin_lyas. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF74650. Gal_mut_like. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF49863. Lyase_like_C. 1 hit.
TIGRFAMsTIGR01167. LPXTG_anchor. 1 hit.
PROSITEPS50847. GRAM_POS_ANCHORING. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00126. Vitamin C.
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Entry informationHide

Entry nameHYSA_STRPN
AccessionPrimary (citable) accession number: Q54873
Secondary accession number(s): Q54874
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 26, 2001
Last modified: June 15, 2010
This is version 94 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 documentsHide

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