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
//