ID   HYSA_CUTAK              Reviewed;         813 AA.
AC   P0CZ01; Q59634; Q6AAT4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Hyaluronate lyase {ECO:0000250|UniProtKB:Q54873};
DE            EC=4.2.2.1 {ECO:0000250|UniProtKB:Q54873};
DE   AltName: Full=Hyaluronidase;
DE            Short=HYase;
DE   Flags: Precursor;
GN   OrderedLocusNames=PPA0380;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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:0000250|UniProtKB:P0CZ00}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC       {ECO:0000305}.
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DR   EMBL; AE017283; AAT82132.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CZ01; -.
DR   SMR; P0CZ01; -.
DR   STRING; 267747.PPA0380; -.
DR   CAZy; PL8; Polysaccharide Lyase Family 8.
DR   EnsemblBacteria; AAT82132; AAT82132; PPA0380.
DR   KEGG; pac:PPA0380; -.
DR   eggNOG; COG5492; Bacteria.
DR   HOGENOM; CLU_004172_4_1_11; -.
DR   OMA; RYYQDET; -.
DR   BRENDA; 4.2.2.1; 5029.
DR   Proteomes; UP000000603; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Lyase; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           33..813
FT                   /note="Hyaluronate lyase"
FT                   /id="PRO_0000024930"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250|UniProtKB:Q54873"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000250|UniProtKB:Q54873"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000250|UniProtKB:Q54873"
SQ   SEQUENCE   813 AA;  88130 MW;  0C4316E7890D4D1D CRC64;
     MFGTPSRRTF LTASALSAMA LAASPTVTDA IAAPGPDSWS ALCERWIDII TGRRAARTSD
     PRARAIIAKT DRKVAEILTD LVSGSSRQTV LISADLRKEQ SPFITKTARA IESMACAWAT
     PGSSYHKDPE ILSACIEGLR DFCRLRYNPS QDEYGNWWDW EDGASRAVAD VMCILHDVLP
     PEVMSAAAAG IDHFIPDPWF QQPASVKPTA NPVQPVVSTG ANRMDLTRAV MCRSIATGDE
     KRLRHAVDGL PDAWRVTTEG DGFRADGGFI QHSHIPYTGG YGDVLFSGLA MLFPLVSGMR
     FDIVESARKA FHDQVERGFI PVMYNGQILD DVRGRSISRI NESAAMHGIS IARAMLMMAD
     ALPTHRAEQW RGIVHGWMAR NTFDHLSEPS TLVDISLFDA AAKARPVPES STPSYFASMD
     RLVHRTADWL ITVSNCSDRI AWYEYGNGEN EWASRTSQGM RYLLLPGDMG QYEDGYWATV
     DYSAPTGTTV DSTPLKRAVG ASWAAKTPTN EWSGGLASGS WSAAASHITS QDSALKARRL
     WVGLKDAMVE LTTDVTTDAS RAITVVEHRK VASSSTKLLV DGNRVSSATS FQNPRWAHLD
     GVGGYVFATD TDLSADVATR KGTWIDVNPS RKVKGADEVI ERAYASLHVT HHDRPVAWAL
     LPTASRSHTM ALATRPGVEP FTVLRNDATV QAVRSAGALL TKDPTVVTTL AFWKPATCGG
     VAVNRPALVQ TRESANQMEV VIVEPTQKRG SLTVTIEGSW KVKTADSHVD VSCENAAGTL
     HVDTAGLGGQ SVRVTLARQV TQTPSGGGRH DRA