ID   HYSA_PROAC              Reviewed;         813 AA.
AC   P0CZ01; Q59634; Q6AAT4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   29-MAY-2013, entry version 15.
DE   RecName: Full=Hyaluronate lyase;
DE            EC=4.2.2.1;
DE   AltName: Full=Hyaluronidase;
DE            Short=HYase;
DE   Flags: Precursor;
GN   OrderedLocusNames=PPA0380;
OS   Propionibacterium acnes (strain KPA171202 / DSM 16379).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Propionibacterineae; Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPA171202 / DSM 16379;
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
RT   of human skin.";
RL   Science 305:671-673(2004).
CC   -!- CATALYTIC ACTIVITY: Cleaves hyaluronate chains at a beta-D-GalNAc-
CC       (1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide
CC       down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-
CC       glucosamine.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall (By similarity).
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
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DR   EMBL; AE017283; AAT82132.1; -; Genomic_DNA.
DR   RefSeq; YP_055090.1; NC_006085.1.
DR   ProteinModelPortal; P0CZ01; -.
DR   EnsemblBacteria; AAT82132; AAT82132; PPA0380.
DR   GeneID; 2932015; -.
DR   KEGG; pac:PPA0380; -.
DR   PATRIC; 23035411; VBIProAcn64440_0390.
DR   HOGENOM; HOG000243554; -.
DR   KO; K01727; -.
DR   OMA; WWHWEIG; -.
DR   BioCyc; PACN267747:GHO9-377-MONOMER; -.
DR   BRENDA; 4.2.2.1; 5029.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
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: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; Glyco_hydro-type_carb-bd_sub.
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; IPR012329; Lyase_8_N.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   SUPFAM; SSF48230; Chondroitin_lyas; 1.
DR   SUPFAM; SSF74650; Gal_mut_like; 1.
DR   SUPFAM; SSF49863; Lyase_like_C; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Cell wall; Complete proteome; Lyase; Secreted; Signal.
FT   SIGNAL        1     32       Tat-type signal (By similarity).
FT   CHAIN        33    813       Hyaluronate lyase.
FT                                /FTId=PRO_0000024930.
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
//