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Q53591

- HYSA_STRA3

UniProt

Q53591 - HYSA_STRA3

Protein

Hyaluronate lyase

Gene

hylB

Organism
Streptococcus agalactiae serotype III (strain NEM316)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (17 Jan 2003)
      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 sitei429 – 4291
    Active sitei479 – 4791
    Active sitei488 – 4881

    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

    BRENDAi4.2.2.1. 5917.

    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
    Name:hylB
    Ordered Locus Names:gbs1270
    OrganismiStreptococcus agalactiae serotype III (strain NEM316)
    Taxonomic identifieri211110 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000823: Chromosome

    Organism-specific databases

    GenoListigbs1270.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4040Sequence AnalysisAdd
    BLAST
    Chaini41 – 984944Hyaluronate lyasePRO_0000024932Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi211110.gbs1270.

    Structurei

    Secondary structure

    1
    984
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi185 – 1884
    Beta strandi196 – 1994
    Beta strandi200 – 2067
    Helixi207 – 2093
    Beta strandi210 – 2134
    Beta strandi216 – 2194
    Beta strandi223 – 2308
    Beta strandi236 – 24510
    Helixi251 – 26313
    Helixi266 – 2683
    Helixi274 – 29320
    Helixi305 – 3073
    Helixi313 – 33018
    Turni336 – 3394
    Helixi341 – 35717
    Beta strandi367 – 3693
    Helixi371 – 3755
    Helixi377 – 38812
    Helixi390 – 3923
    Helixi395 – 40814
    Beta strandi414 – 4163
    Turni417 – 4204
    Helixi427 – 44317
    Helixi447 – 45711
    Helixi458 – 4603
    Beta strandi464 – 4718
    Beta strandi476 – 4783
    Turni479 – 4813
    Turni485 – 4873
    Helixi488 – 50316
    Helixi512 – 52413
    Helixi527 – 5293
    Helixi537 – 5393
    Helixi541 – 5455
    Helixi551 – 56616
    Helixi572 – 58716
    Beta strandi589 – 5913
    Helixi593 – 5964
    Helixi600 – 61112
    Beta strandi623 – 6275
    Helixi628 – 6303
    Beta strandi632 – 6376
    Turni638 – 6414
    Beta strandi642 – 6476
    Beta strandi653 – 6553
    Beta strandi660 – 6623
    Turni667 – 6704
    Beta strandi671 – 6777
    Turni681 – 6844
    Beta strandi685 – 6873
    Helixi688 – 6914
    Beta strandi694 – 6963
    Beta strandi701 – 7033
    Helixi712 – 7165
    Turni717 – 7204
    Helixi722 – 7265
    Beta strandi736 – 75318
    Beta strandi757 – 76812
    Beta strandi771 – 78111
    Beta strandi782 – 7843
    Beta strandi788 – 7969
    Beta strandi799 – 8013
    Beta strandi804 – 8074
    Beta strandi816 – 83116
    Beta strandi839 – 85820
    Helixi860 – 8634
    Beta strandi873 – 88311
    Beta strandi886 – 8883
    Beta strandi891 – 8988
    Helixi901 – 9099
    Beta strandi912 – 9187
    Beta strandi920 – 9278
    Turni928 – 9314
    Beta strandi932 – 9376
    Beta strandi943 – 9453
    Turni946 – 9483
    Beta strandi949 – 9513
    Beta strandi955 – 9628
    Beta strandi965 – 9728
    Turni973 – 9764
    Beta strandi977 – 9815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F1SX-ray2.10A171-984[»]
    1I8QX-ray2.20A171-984[»]
    1LXMX-ray2.20A171-984[»]
    ProteinModelPortaliQ53591.
    SMRiQ53591. Positions 171-984.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53591.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polysaccharide lyase 8 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG305085.
    HOGENOMiHOG000008667.
    KOiK01727.
    OrthoDBiEOG6GBM67.

    Family and domain databases

    Gene3Di1.50.10.100. 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.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q53591-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKQVVDNQTQ NKELVKNGDF NQTNPVSGSW SHTSAREWSA WIDKENTADK    50
    SPIIQRTEQG QVSLSSDKGF RGAVTQKVNI DPTKKYEVKF DIETSNKAGQ 100
    AFLRIMEKKD NNTRLWLSEM TSGTTNKHTL TKIYNPKLNV SEVTLELYYE 150
    KGTGSATFDN ISMKAKGPKD SEHPQPVTTQ IEESVNTALN KNYVFNKADY 200
    QYTLTNPSLG KIVGGILYPN ATGSTTVKIS DKSGKIIKEV PLSVTASTED 250
    KFTKLLDKWN DVTIGNHVYD TNDSNMQKIN QKLDETNAKN IKTIKLDSNH 300
    TFLWKDLDNL NNSAQLTATY RRLEDLAKQI TNPHSTIYKN EKAIRTVKES 350
    LAWLHQNFYN VNKDIEGSAN WWDFEIGVPR SITATLALMN NYFTDAEIKT 400
    YTDPIEHFVP DAGYFRKTLD NPFKALGGNL VDMGRVKIIE GLLRKDNTII 450
    EKTSHSLKNL FTTATKAEGF YADGSYIDHT NVAYTGAYGN VLIDGLTQLL 500
    PIIQETDYKI SNQELDMVYK WINQSFLPLI VKGELMDMSR GRSISREAAS 550
    SHAAAVEVLR GFLRLANMSN EERNLDLKST IKTIITSNKF YNVFNNLKSY 600
    SDIANMNKML NDSTVATKPL KSNLSTFNSM DRLAYYNAEK DFGFALSLHS 650
    KRTLNYEGMN DENTRDWYTG DGMFYLYNSD QSHYSNHFWP TVNPYKMAGT 700
    TEKDAKREDT TKEFMSKHSK DAKEKTGQVT GTSDFVGSVK LNDHFALAAM 750
    DFTNWDRTLT AQKGWVILND KIVFLGSNIK NTNGIGNVST TIDQRKDDSK 800
    TPYTTYVNGK TIDLKQASSQ QFTDTKSVFL ESKEPGRNIG YIFFKNSTID 850
    IERKEQTGTW NSINRTSKNT SIVSNPFITI SQKHDNKGDS YGYMMVPNID 900
    RTSFDKLANS KEVELLENSS KQQVIYDKNS QTWAVIKHDN QESLINNQFK 950
    MNKAGLYLVQ KVGNDYQNVY YQPQTMTKTD QLAI 984
    Length:984
    Mass (Da):111,581
    Last modified:January 17, 2003 - v2
    Checksum:iAC7215ED6D5C2592
    GO

    Sequence cautioni

    The sequence CAD46929.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451E → G in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti155 – 1562SA → FV in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti183 – 1831E → K in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti246 – 2516ASTEDK → GSPEDN in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti267 – 2671H → Y in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti279 – 2802IN → LT in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti288 – 2881A → G in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti292 – 2932KT → EA in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti300 – 3001H → R in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti384 – 3841A → G in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti387 – 3871A → S in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti413 – 4131G → E in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti420 – 4201D → V in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti583 – 5831T → A in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti609 – 6091M → L in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti639 – 6391E → K in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti666 – 6661D → G in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti676 – 6761L → I in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti688 – 6892FW → LG in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti882 – 8821Q → L in AAA56749. (PubMed:7982914)Curated
    Sequence conflicti894 – 8941M → L in AAA56749. (PubMed:7982914)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15050 Genomic DNA. Translation: AAA56749.1.
    AL766849 Genomic DNA. Translation: CAD46929.1. Different initiation.
    PIRiA55137.
    RefSeqiNP_735714.1. NC_004368.1.

    Genome annotation databases

    EnsemblBacteriaiCAD46929; CAD46929; CAD46929.
    GeneIDi1030294.
    KEGGisan:gbs1270.
    PATRICi19638423. VBIStrAga3577_1300.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15050 Genomic DNA. Translation: AAA56749.1 .
    AL766849 Genomic DNA. Translation: CAD46929.1 . Different initiation.
    PIRi A55137.
    RefSeqi NP_735714.1. NC_004368.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F1S X-ray 2.10 A 171-984 [» ]
    1I8Q X-ray 2.20 A 171-984 [» ]
    1LXM X-ray 2.20 A 171-984 [» ]
    ProteinModelPortali Q53591.
    SMRi Q53591. Positions 171-984.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 211110.gbs1270.

    Protein family/group databases

    CAZyi PL8. Polysaccharide Lyase Family 8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD46929 ; CAD46929 ; CAD46929 .
    GeneIDi 1030294.
    KEGGi san:gbs1270.
    PATRICi 19638423. VBIStrAga3577_1300.

    Organism-specific databases

    GenoListi gbs1270.

    Phylogenomic databases

    eggNOGi NOG305085.
    HOGENOMi HOG000008667.
    KOi K01727.
    OrthoDBi EOG6GBM67.

    Enzyme and pathway databases

    BRENDAi 4.2.2.1. 5917.

    Miscellaneous databases

    EvolutionaryTracei Q53591.

    Family and domain databases

    Gene3Di 1.50.10.100. 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.
    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.
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NEM316.
    3. "Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase."
      Li S., Jedrzejas M.J.
      J. Biol. Chem. 276:41407-41416(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 171-984.

    Entry informationi

    Entry nameiHYSA_STRA3
    AccessioniPrimary (citable) accession number: Q53591
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 17, 2003
    Last modified: October 1, 2014
    This is version 101 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