ID   C0MDA1_STRS7            Unreviewed;      1063 AA.
AC   C0MDA1;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 90.
DE   SubName: Full=Hyaluronate lyase {ECO:0000313|EMBL:CAW98747.1};
GN   OrderedLocusNames=SZO_06680 {ECO:0000313|EMBL:CAW98747.1};
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483 {ECO:0000313|EMBL:CAW98747.1, ECO:0000313|Proteomes:UP000001368};
RN   [1] {ECO:0000313|EMBL:CAW98747.1, ECO:0000313|Proteomes:UP000001368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70 {ECO:0000313|EMBL:CAW98747.1,
RC   ECO:0000313|Proteomes:UP000001368};
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC       {ECO:0000256|ARBA:ARBA00006699}.
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DR   EMBL; FM204884; CAW98747.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MDA1; -.
DR   KEGG; seq:SZO_06680; -.
DR   eggNOG; COG5492; Bacteria.
DR   HOGENOM; CLU_004172_0_0_9; -.
DR   Proteomes; UP000001368; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-ARBA.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 2.60.40.1380; E set domains, domain 4; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 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; IPR023295; Hyaluronate_lyase_beta_dom_sf.
DR   InterPro; IPR054563; HylB-like_N.
DR   InterPro; IPR014756; Ig_E-set.
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; HYALURONATE LYASE; 1.
DR   PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR   Pfam; PF22637; CBM_4_9_1; 1.
DR   Pfam; PF21461; HL_N-beta; 1.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAW98747.1};
KW   Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001368};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PROSITE-
KW   ProRule:PRU00303}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1063
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_5049189349"
FT   CHAIN           29..1063
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002900560"
FT   DOMAIN          87..244
FT                   /note="Hyaluronate lyase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF22637"
FT   DOMAIN          268..327
FT                   /note="Hyaluronate lyase N-terminal beta-sheet"
FT                   /evidence="ECO:0000259|Pfam:PF21461"
FT   DOMAIN          342..668
FT                   /note="Polysaccharide lyase 8 N-terminal alpha-helical"
FT                   /evidence="ECO:0000259|Pfam:PF08124"
FT   DOMAIN          711..994
FT                   /note="Polysaccharide lyase family 8 central"
FT                   /evidence="ECO:0000259|Pfam:PF02278"
FT   DOMAIN          1002..1054
FT                   /note="Polysaccharide lyase family 8 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02884"
FT   REGION          39..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638970-1"
FT   ACT_SITE        574
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638970-1"
FT   ACT_SITE        628
FT                   /evidence="ECO:0000256|PIRSR:PIRSR638970-1"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   1063 AA;  119322 MW;  71F29291F6E32C5F CRC64;
     MKQRKKLSSS VCSSIILACL FRAPTVLAEE KTAAKAISKE LQRVKKAPLK TEEASQESSP
     DTQDASSVAT ESSLGEQLIL TGDNLLKNPQ FDQTSPAQEH QSTSLWSKES ANDWKDYKDA
     SKSQGCPKIA VSDNKLTMTS DGNQRFRGCV HQTVAINPDK QYLLTFDIET KDKTGQAFAR
     IIEEIKQGSG AAKEQRLWLS PMATGTEKKH QEKLYIPKLK VNQIKLELFY EAGHGQVVFD
     NLSLREAGDK PSDDIKIASH YLEEQIVLPL NKHYLMEMAD YHYQIAAESS NIVRVENGLL
     IPLAQGKTLL EVLDQEGQRV VTVPVEILAA EDPQTTSLIT KWCEVILGAE NFDRSSPAMV
     ALNQKLDDSV TKNLAVLTKD QKSTYLWSDL ADLHQSSHMT ATCRRLEEMA KQVSSLASRY
     YQDKELIRLI KDKLAWLTLN YYHPQKDIEG KANWWDFEIG TPRAIVNTLA FLYPYVTQEE
     IKRYTKGISH FVPNPRQFRS TLVNPFKAIG GNLVDMGRIK IIEALLRHDK KALQDSIAAL
     DTLFAFQPRG SKGEGFYEDG SYIDHTNVAY TGAYGNVLID GLSQLVPLIQ QSAASLDQKK
     LEAMTHWIEQ AFLPLMVHGE LMDMNRGRSI SRENASSRQA ALEALRGMLR LADALPEQAK
     IRVKGKIKAV LAFHNQEAIL ESLSSYYDMK LFKELLEDTA IQASPVKSYL SLFNQMDKLA
     YYNAEKDFAF ALSLHSNKTL NFEAMNNENT RGWYTGDGMF YLYNSDLGHY SDRFWPTVNP
     LKMAGTTEAE VHREDVTVAY LKKLTNDYKE KAKEKAGMST QQSSFVGAIK AGDKTALAVM
     DFQNWDRTVS AKKSWTILDD QIVFLGTAIT SQTHQAVTTT IDQRKENPDN SYILFINGQE
     TALTEEVLHR DDVTSLLLLS KDGQANIGYL FAKPTALALS RKVQSGCWSE INTNSNNKDL
     ISQSFITISQ THSQASDSYA YTLLPNISKA DFDKVCSEAR IEVLRNDSKL QLIHDKKQGL
     LAVVKYNQAK EVVNGQLSLE KSGLYLYQKV GNDFKQLSFK ALS
//