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Q54873

- HYSA_STRPN

UniProt

Q54873 - HYSA_STRPN

Protein

Hyaluronate lyase

Gene

SP_0314

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei466 – 4661
    Active sitei516 – 5161
    Active sitei525 – 5251

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. hyaluronate lyase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Enzyme and pathway databases

    BioCyciSPNE170187:GHGN-320-MONOMER.
    BRENDAi4.2.2.1. 5946.
    SABIO-RKQ54873.

    Protein family/group databases

    CAZyiPL8. Polysaccharide Lyase Family 8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hyaluronate lyase (EC:4.2.2.1)
    Alternative name(s):
    Hyaluronidase
    Short name:
    HYase
    Gene namesi
    Ordered Locus Names:SP_0314
    OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
    Taxonomic identifieri170187 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000585: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell wall, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi360 – 3601R → V: Retains 67% of wild-type activity. 1 Publication
    Mutagenesisi466 – 4661N → A: Almost complete loss of activity. 1 Publication
    Mutagenesisi516 – 5161H → A: Almost complete loss of activity. 1 Publication
    Mutagenesisi525 – 5251Y → F: Complete loss of activity. 1 Publication
    Mutagenesisi697 – 6971N → G: Slightly increased activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 10391009Hyaluronate lyasePRO_0000024933Add
    BLAST
    Propeptidei1040 – 106627Removed by sortaseSequence AnalysisPRO_0000024934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1039 – 10391Pentaglycyl murein peptidoglycan amidated threonineSequence Analysis

    Keywords - PTMi

    Peptidoglycan-anchor

    Proteomic databases

    PRIDEiQ54873.

    Interactioni

    Protein-protein interaction databases

    STRINGi170187.SP_0314.

    Structurei

    Secondary structure

    1
    1066
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi290 – 30213
    Helixi305 – 3073
    Beta strandi310 – 3123
    Helixi313 – 33220
    Beta strandi336 – 3383
    Beta strandi340 – 3423
    Helixi344 – 3463
    Beta strandi349 – 3513
    Helixi353 – 36917
    Turni375 – 3784
    Helixi380 – 39617
    Beta strandi398 – 4014
    Helixi408 – 4125
    Helixi414 – 42512
    Helixi427 – 4293
    Helixi432 – 44514
    Beta strandi451 – 4533
    Beta strandi456 – 4583
    Helixi464 – 48017
    Helixi484 – 49411
    Helixi495 – 4984
    Beta strandi502 – 5076
    Beta strandi513 – 5153
    Turni516 – 5183
    Turni522 – 5243
    Helixi525 – 54016
    Beta strandi543 – 5453
    Helixi549 – 5524
    Helixi554 – 5618
    Helixi564 – 5663
    Helixi574 – 5763
    Helixi578 – 5825
    Helixi584 – 5863
    Helixi588 – 60518
    Helixi608 – 62417
    Beta strandi626 – 6283
    Helixi630 – 6334
    Helixi637 – 64812
    Beta strandi660 – 6645
    Helixi665 – 6673
    Beta strandi669 – 6746
    Turni675 – 6784
    Beta strandi679 – 6846
    Beta strandi690 – 6923
    Turni704 – 7074
    Beta strandi711 – 7144
    Turni718 – 7214
    Helixi725 – 7284
    Helixi731 – 7333
    Beta strandi738 – 7403
    Beta strandi758 – 7603
    Beta strandi767 – 7759
    Beta strandi779 – 78911
    Beta strandi794 – 80310
    Beta strandi805 – 8073
    Beta strandi809 – 8179
    Beta strandi820 – 8223
    Beta strandi825 – 8284
    Beta strandi831 – 8333
    Beta strandi840 – 85112
    Helixi855 – 8573
    Beta strandi859 – 87820
    Helixi880 – 8823
    Beta strandi892 – 90211
    Beta strandi908 – 91710
    Helixi920 – 92910
    Turni930 – 9323
    Beta strandi934 – 94613
    Turni947 – 9504
    Beta strandi951 – 9588
    Beta strandi962 – 9643
    Turni965 – 9673
    Beta strandi968 – 9703
    Beta strandi972 – 98110
    Beta strandi984 – 9918
    Turni992 – 9954
    Helixi1000 – 10034
    Beta strandi1004 – 10063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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-ray1.78A291-1009[»]
    1OJNX-ray1.60A285-1009[»]
    1OJOX-ray1.75A285-1009[»]
    1OJPX-ray1.90A285-1009[»]
    1W3YX-ray1.65A285-1009[»]
    2BRPX-ray2.00A285-1009[»]
    2BRVX-ray3.30X285-1009[»]
    2BRWX-ray2.80A/B285-1009[»]
    ProteinModelPortaliQ54873.
    SMRiQ54873. Positions 212-1008.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ54873.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1036 – 10405LPXTG sorting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the polysaccharide lyase 8 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG04835.
    HOGENOMiHOG000008667.
    KOiK01727.
    OMAiRYYQDET.
    OrthoDBiEOG6GBM67.

    Family and domain databases

    Gene3Di1.50.10.100. 1 hit.
    2.60.120.260. 1 hit.
    2.60.220.10. 1 hit.
    2.60.40.1380. 1 hit.
    2.70.98.10. 1 hit.
    InterProiIPR008929. Chondroitin_lyas.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR008979. Galactose-bd-like.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR023295. Hyaluronate_lyase_beta_dom.
    IPR014756. Ig_E-set.
    IPR019931. LPXTG_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]
    PfamiPF02278. Lyase_8. 1 hit.
    PF02884. Lyase_8_C. 1 hit.
    PF08124. Lyase_8_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48230. SSF48230. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF49863. SSF49863. 1 hit.
    SSF74650. SSF74650. 1 hit.
    SSF81296. SSF81296. 1 hit.
    TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q54873-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQTKTKKLIV SLSSLVLSGF LLNHYMTIGA EETTTNTIQQ SQKEVQYQQR     50
    DTKNLVENGD FGQTEDGSSP WTGSKAQGWS AWVDQKNSAD ASTRVIEAKD 100
    GAITISSHEK LRAALHRMVP IEAKKKYKLR FKIKTDNKIG IAKVRIIEES 150
    GKDKRLWNSA TTSGTKDWQT IEADYSPTLD VDKIKLELFY ETGTGTVSFK 200
    DIELVEVADQ LSEDSQTDKQ LEEKIDLPIG KKHVFSLADY TYKVENPDVA 250
    SVKNGILEPL KEGTTNVIVS KDGKEVKKIP LKILASVKDA YTDRLDDWNG 300
    IIAGNQYYDS KNEQMAKLNQ ELEGKVADSL SSISSQADRT YLWEKFSNYK 350
    TSANLTATYR KLEEMAKQVT NPSSRYYQDE TVVRTVRDSM EWMHKHVYNS 400
    EKSIVGNWWD YEIGTPRAIN NTLSLMKEYF SDEEIKKYTD VIEKFVPDPE 450
    HFRKTTDNPF KALGGNLVDM GRVKVIAGLL RKDDQEISST IRSIEQVFKL 500
    VDQGEGFYQD GSYIDHTNVA YTGAYGNVLI DGLSQLLPVI QKTKNPIDKD 550
    KMQTMYHWID KSFAPLLVNG ELMDMSRGRS ISRANSEGHV AAVEVLRGIH 600
    RIADMSEGET KQCLQSLVKT IVQSDSYYDV FKNLKTYKDI SLMQSLLSDA 650
    GVASVPRPSY LSAFNKMDKT AMYNAEKGFG FGLSLFSSRT LNYEHMNKEN 700
    KRGWYTSDGM FYLYNGDLSH YSDGYWPTVN PYKMPGTTET DAKRADSDTG 750
    KVLPSAFVGT SKLDDANATA TMDFTNWNQT LTAHKSWFML KDKIAFLGSN 800
    IQNTSTDTAA TTIDQRKLES GNPYKVYVND KEASLTEQEK DYPETQSVFL 850
    ESFDSKKNIG YFFFKKSSIS MSKALQKGAW KDINEGQSDK EVENEFLTIS 900
    QAHKQNRDSY GYMLIPNVDR ATFNQMIKEL ESSLIENNET LQSVYDAKQG 950
    VWGIVKYDDS VSTISNQFQV LKRGVYTIRK EGDEYKIAYY NPETQESAPD 1000
    QEVFKKLEQA AQPQVQNSKE KEKSEEEKNH SDQKNLPQTG EGQSILASLG 1050
    FLLLGAFYLF RRGKNN 1066
    Length:1,066
    Mass (Da):120,771
    Last modified:September 26, 2001 - v2
    Checksum:i81DB22A837BE61F9
    GO

    Sequence cautioni

    The sequence AAA53685.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAA53686.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081H → P(PubMed:8112843)Curated
    Sequence conflicti115 – 1151L → V(PubMed:8112843)Curated
    Sequence conflicti139 – 1391I → V in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti211 – 2111L → P in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti236 – 2361S → P in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti290 – 2901A → T in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti290 – 2901A → T in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti313 – 3131E → D in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti313 – 3131E → D in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti340 – 3401T → I in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti340 – 3401T → I in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti613 – 6131C → R in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti613 – 6131C → R in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti658 – 6581P → T in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti658 – 6581P → T in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti821 – 8211G → S in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti821 – 8211G → S in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti848 – 8481V → G in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti848 – 8481V → G in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti853 – 8531F → S in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti853 – 8531F → S in AAA53686. (PubMed:8112843)Curated
    Sequence conflicti907 – 9071R → G in AAA53685. (PubMed:8112843)Curated
    Sequence conflicti907 – 9071R → G in AAA53686. (PubMed:8112843)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005672 Genomic DNA. Translation: AAK74491.1.
    L20670 Genomic DNA. Translation: AAA53685.1. Different initiation.
    L20670 Genomic DNA. Translation: AAA53686.1. Different initiation.
    PIRiB95037.
    RefSeqiNP_344851.1. NC_003028.3.
    WP_001193686.1. NZ_AKVY01000001.1.

    Genome annotation databases

    EnsemblBacteriaiAAK74491; AAK74491; SP_0314.
    GeneIDi930127.
    KEGGispn:SP_0314.
    PATRICi19704965. VBIStrPne105772_0328.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005672 Genomic DNA. Translation: AAK74491.1 .
    L20670 Genomic DNA. Translation: AAA53685.1 . Different initiation.
    L20670 Genomic DNA. Translation: AAA53686.1 . Different initiation.
    PIRi B95037.
    RefSeqi NP_344851.1. NC_003028.3.
    WP_001193686.1. NZ_AKVY01000001.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C82 X-ray 1.70 A 285-1009 [» ]
    1EGU X-ray 1.56 A 285-1009 [» ]
    1F9G X-ray 2.00 A 285-1009 [» ]
    1LOH X-ray 2.00 A 287-1007 [» ]
    1LXK X-ray 1.53 A 287-1007 [» ]
    1N7N X-ray 1.55 A 287-1007 [» ]
    1N7O X-ray 1.50 A 287-1007 [» ]
    1N7P X-ray 1.55 A 287-1007 [» ]
    1N7Q X-ray 2.30 A 287-1007 [» ]
    1N7R X-ray 2.20 A 287-1007 [» ]
    1OJM X-ray 1.78 A 291-1009 [» ]
    1OJN X-ray 1.60 A 285-1009 [» ]
    1OJO X-ray 1.75 A 285-1009 [» ]
    1OJP X-ray 1.90 A 285-1009 [» ]
    1W3Y X-ray 1.65 A 285-1009 [» ]
    2BRP X-ray 2.00 A 285-1009 [» ]
    2BRV X-ray 3.30 X 285-1009 [» ]
    2BRW X-ray 2.80 A/B 285-1009 [» ]
    ProteinModelPortali Q54873.
    SMRi Q54873. Positions 212-1008.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 170187.SP_0314.

    Chemistry

    BindingDBi Q54873.
    ChEMBLi CHEMBL1795158.
    DrugBanki DB00126. Vitamin C.

    Protein family/group databases

    CAZyi PL8. Polysaccharide Lyase Family 8.

    Proteomic databases

    PRIDEi Q54873.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK74491 ; AAK74491 ; SP_0314 .
    GeneIDi 930127.
    KEGGi spn:SP_0314.
    PATRICi 19704965. VBIStrPne105772_0328.

    Phylogenomic databases

    eggNOGi NOG04835.
    HOGENOMi HOG000008667.
    KOi K01727.
    OMAi RYYQDET.
    OrthoDBi EOG6GBM67.

    Enzyme and pathway databases

    BioCyci SPNE170187:GHGN-320-MONOMER.
    BRENDAi 4.2.2.1. 5946.
    SABIO-RK Q54873.

    Miscellaneous databases

    EvolutionaryTracei Q54873.

    Family and domain databases

    Gene3Di 1.50.10.100. 1 hit.
    2.60.120.260. 1 hit.
    2.60.220.10. 1 hit.
    2.60.40.1380. 1 hit.
    2.70.98.10. 1 hit.
    InterProi IPR008929. Chondroitin_lyas.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR008979. Galactose-bd-like.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR023295. Hyaluronate_lyase_beta_dom.
    IPR014756. Ig_E-set.
    IPR019931. LPXTG_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 ]
    Pfami PF02278. Lyase_8. 1 hit.
    PF02884. Lyase_8_C. 1 hit.
    PF08124. Lyase_8_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48230. SSF48230. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF49863. SSF49863. 1 hit.
    SSF74650. SSF74650. 1 hit.
    SSF81296. SSF81296. 1 hit.
    TIGRFAMsi TIGR01167. LPXTG_anchor. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

    Entry informationi

    Entry nameiHYSA_STRPN
    AccessioniPrimary (citable) accession number: Q54873
    Secondary accession number(s): Q54874
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3