ID   HYSA_STAA8              Reviewed;         807 AA.
AC   Q59801; Q2FW54;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Hyaluronate lyase {ECO:0000303|PubMed:7557301};
DE            EC=4.2.2.1 {ECO:0000250|UniProtKB:Q54873};
DE   AltName: Full=Hyaluronidase;
DE            Short=HYase;
DE   Flags: Precursor;
GN   Name=hysA {ECO:0000303|PubMed:7557301}; OrderedLocusNames=SAOUHSC_02463;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7557301; DOI=10.1111/j.1574-6968.1995.tb07702.x;
RA   Farrell A.M., Taylor D., Holland K.T.;
RT   "Cloning, nucleotide sequence determination and expression of the
RT   Staphylococcus aureus hyaluronate lyase gene.";
RL   FEMS Microbiol. Lett. 130:81-85(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[hyaluronan](n) = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-
CC         acetyl-D-glucosamine + H2O; Xref=Rhea:RHEA:50240, Rhea:RHEA-
CC         COMP:12583, ChEBI:CHEBI:15377, ChEBI:CHEBI:132151,
CC         ChEBI:CHEBI:132153; EC=4.2.2.1;
CC         Evidence={ECO:0000250|UniProtKB:Q54873};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U21221; AAA82984.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD31483.1; -; Genomic_DNA.
DR   RefSeq; WP_000222239.1; NZ_LS483365.1.
DR   RefSeq; YP_500931.1; NC_007795.1.
DR   AlphaFoldDB; Q59801; -.
DR   SMR; Q59801; -.
DR   STRING; 1280.SAXN108_2455; -.
DR   CAZy; PL8; Polysaccharide Lyase Family 8.
DR   PRIDE; Q59801; -.
DR   EnsemblBacteria; ABD31483; ABD31483; SAOUHSC_02463.
DR   GeneID; 3919026; -.
DR   KEGG; sao:SAOUHSC_02463; -.
DR   PATRIC; fig|93061.5.peg.2222; -.
DR   eggNOG; COG5492; Bacteria.
DR   HOGENOM; CLU_004172_5_1_9; -.
DR   OMA; RYYQDET; -.
DR   BRENDA; 4.2.2.1; 3352.
DR   PRO; PR:Q59801; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0030340; F:hyaluronate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.100; -; 1.
DR   Gene3D; 2.60.220.10; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR038970; Lyase_8.
DR   InterPro; IPR011071; Lyase_8-like_C.
DR   InterPro; IPR012970; Lyase_8_alpha_N.
DR   InterPro; IPR004103; Lyase_8_C.
DR   InterPro; IPR003159; Lyase_8_central_dom.
DR   PANTHER; PTHR38481; PTHR38481; 1.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   SUPFAM; SSF48230; SSF48230; 1.
DR   SUPFAM; SSF49863; SSF49863; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..807
FT                   /note="Hyaluronate lyase"
FT                   /id="PRO_0000024931"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000250|UniProtKB:Q54873"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250|UniProtKB:Q54873"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000250|UniProtKB:Q54873"
SQ   SEQUENCE   807 AA;  91985 MW;  FFE88EDC07418EB4 CRC64;
     MTYRIKKWQK LSTITLLMAG VITLNGGEFR SVDKHQIAVA DTNVQTPDYE KLRNTWLDVN
     YGYDKYDENN PDMKKKFDAT EKEATNLLKE MKTESGRKYL WSGAETLETN SSHMTRTYRN
     IEKIAEAMRN PKTTLNTDEN KKKVKDALEW LHKNAYGKEP DKKVKELSEN FTKTTGKNTN
     LNWWDYEIGT PKSLTNTLIL LNDQFSNEEK KKFTAPIKTF APDSDKILSS VGKAELAKGG
     NLVDISKVKL LECIIEEDKD MMKKSIDSFN KVFTYVQDSA TGKERNGFYK DGSYIDHQDV
     PYTGAYGVVL LEGISQMMPM IKETPFNDKT QNDTTLKSWI DDGFMPLIYK GEMMDLSRGR
     AISRENETSH SASATVMKSL LRLSDAMDDS TKAKYKKIVK SSVESDSSYK QNDYLNSYSD
     IDKMKSLMTD NSISKNGLTQ QLKIYNDMDR VTYHNKDLDF AFGLSMTSKN VARYESINGE
     NLKGWHTGAG MSYLYNSDVK HYHDNFWVTA DMKRLSGTTT LDNEILKDTD DKKSSKTFVG
     GTKVDDQHAS IGMDFENQDK TLTAKKSYFI LNDKIVFLGT GIKSTDSSKN PVTTIENRKA
     NGYTLYTDDK QTTNSDNQEN NSVFLESTDT KKNIGYHFLN KPKITVKKES HTGKWKEINK
     SQKDTQKTDE YYEVTQKHSN SDNKYGYVLY PGLSKDVFKT KKDEVTVVKQ EDDFHVVKDN
     ESVWAGVNYS NSTQTFDINN TKVEVKAKGM FILKKKDDNT YECSFYNPES TNSASDIESK
     ISMTGYSITN KNTSTSNESG VHFELTK