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Database: UniProt
Entry: A4ZX85_STRSU
LinkDB: A4ZX85_STRSU
Original site: A4ZX85_STRSU 
ID   A4ZX85_STRSU            Unreviewed;       940 AA.
AC   A4ZX85;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Hyaluronidase {ECO:0000313|EMBL:ABP35952.1};
GN   Name=hylA {ECO:0000313|EMBL:ABP35952.1};
OS   Streptococcus suis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1307 {ECO:0000313|EMBL:ABP35952.1};
RN   [1] {ECO:0000313|EMBL:ABP35952.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cvcc607 {ECO:0000313|EMBL:ABP35952.1};
RA   Wang J.F., Ran X.Q., Feng Y.L.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC       {ECO:0000256|ARBA:ARBA00006699}.
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DR   EMBL; EF492987; ABP35952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4ZX85; -.
DR   CAZy; CBM70; Carbohydrate-Binding Module Family 70.
DR   CAZy; PL8; Polysaccharide Lyase Family 8.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   CDD; cd01083; GAG_Lyase; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR048734; HL_N-beta.
DR   InterPro; IPR038970; Lyase_8.
DR   InterPro; IPR012970; Lyase_8_alpha_N.
DR   InterPro; IPR003159; Lyase_8_central_dom.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   NCBIfam; TIGR01168; YSIRK_signal; 1.
DR   PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR   PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR   Pfam; PF21461; HL_N-beta; 1.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          8..32
FT                   /note="YSIRK Gram-positive signal peptide"
FT                   /evidence="ECO:0000259|Pfam:PF04650"
FT   DOMAIN          293..342
FT                   /note="Hyaluronate lyase N-terminal beta-sheet"
FT                   /evidence="ECO:0000259|Pfam:PF21461"
FT   DOMAIN          364..685
FT                   /note="Polysaccharide lyase 8 N-terminal alpha-helical"
FT                   /evidence="ECO:0000259|Pfam:PF08124"
FT   DOMAIN          729..932
FT                   /note="Polysaccharide lyase family 8 central"
FT                   /evidence="ECO:0000259|Pfam:PF02278"
FT   REGION          73..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   940 AA;  105232 MW;  A57CE9251DD62253 CRC64;
     MGFFISQSKQ HYGIRKYKVG VCSALIALSI LGTRVAANQL PSTETASPQS SQLVETTPET
     TEAVNLTTEA VMTSEVSSEV SPVTSTETQP SSTAAETLAS PQAVQATKEE EKNLVANGEF
     ASTTAASGNW ADPAATNWET WIPANVKKEN GQVRIDEGRL HISSTASYRV AVHQTVDVDP
     NKRYLFSYNV ETKDLKGSGV RVRLRSLTAE GKDLSPQEFA YTPYKNGSQA EHIEQILTVS
     PETRKLKVEL FFENSVGQAW LDNISLVEYV EKTPETPEPS LELVQPETGQ ISLASNKVYL
     PVRPDLTYRI ADAAVAIVEK NMIRPLAAGK TQVDVYDKDT KLSSFELTVT EHQATVFDTL
     RNNWEDISLA NKRYQSNDTQ MKAFLGRLGA GVASSLKKWV EPTNQGKTIF NDIDFSKSSH
     LTTVYRRLEQ MAQVVENPDS AYYHDRSLID LVRKGMNWLY TNVYNENKSI DGNWWDYEIG
     TPRVVVNTLI YMHPYFSQEE ILTYIKPISK FVPDPTTIRK TLTNPVPAVG GNQTDLSKVA
     ILEGALREDA DRVRAGAQGL TTIMKFVDKG EGFYKDGSFI DHTNVAYTGA YGNVLIEGFS
     QLLPVIQPTE FALKEEQTNI LYEWIEKAFM PILVRGELMD MTRGRSISRA TGESHVQAME
     ILRSLVRIAE SAQPEQKNKL LSFVKAQLTS DTFYDSYRSL KSYKDIDLVN KLLADNQISA
     EADKDYIAAF NNMDKFVYRS AQEGFTFALS MYSSKTQNYE DMNNENRKGW YTADGMVYLY
     SDDLSHYSNH YWATVDPYRL PGTTTTKDKR EDGSGEVTLA SDFVGASQLG NRLATIAMNF
     NNWNNSLTAR KAWIVLGNKI VFLGTDIQHQ SAQGAVTTIE NRKLLTGEKY SYYINGQPVD
     LSKEVVTDKT QSFYMTNGKD NQSIGYVFLN QLPTYAKLDQ
//
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