ID   PRZN_RENSA              Reviewed;         548 AA.
AC   P55111;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Zinc metalloproteinase;
DE            EC=3.4.24.-;
DE   AltName: Full=Hemolysin;
DE   Flags: Precursor;
GN   Name=hly;
OS   Renibacterium salmoninarum.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX   NCBI_TaxID=1646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT444;
RX   PubMed=7545509; DOI=10.1099/13500872-141-6-1331;
RA   Grayson T.H., Evenden A.J., Gilpin M.L., Martin K.L., Munn C.B.;
RT   "A gene from Renibacterium salmoninarum encoding a product which shows
RT   homology to bacterial zinc-metalloproteases.";
RL   Microbiology 141:1331-1341(1995).
RN   [2]
RP   SEQUENCE REVISION TO 149-170.
RA   Grayson T.H.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc metalloprotease with hemolytic properties.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Hemolytic activity is observed from 6 to 37 degrees Celsius for
CC         mammalian erythrocytes.;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Note=Not secreted, but
CC       probably remains attached or associated with the cell wall.
CC   -!- INDUCTION: Expression of the hemolysin is modulated by the availability
CC       of iron.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; X76499; CAA54032.2; -; Genomic_DNA.
DR   RefSeq; WP_012246528.1; NZ_CP029237.1.
DR   AlphaFoldDB; P55111; -.
DR   SMR; P55111; -.
DR   OMA; RHETIRT; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell wall; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028618"
FT   CHAIN           ?..548
FT                   /note="Zinc metalloproteinase"
FT                   /id="PRO_0000028619"
FT   REGION          440..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        459
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   548 AA;  56379 MW;  7AD090DD7425B90A CRC64;
     MKKYYAVTGI ALAVGMLCTT QLAGATQAAD PSVGSLDSSN VVTEFSAQGN VEQITFKSAI
     KSAPMSSARS AQTSAIIPGL KNLFVSAPGS DFSLNDSSNN YIKRFTQNIA GIPVLGSSIT
     EVLDGQGAVT SAIGAVTSAT KGAFPADLAA GQAAALASAT KIASAGKDAS AISLVDQKAI
     WFDAVLIGKG ATGSVAVPAY QFSFTTGFAE SRVLTVAAND GAILNDRTDR KDINRVVCDA
     NSKVIDLEAS NADALLKCGK TQANKPTRIE GQAASSVADV NSVYNFLNDT ASFYGANTKA
     NDLTALIGND EGDGLGKAMR AVVRICVTDS QNGEQCPFAN AFWYNGQMTY GQGVTTDDIT
     GHELTHGVTE KTNGLVYANE SGAINESMSD VFGEFIDLSN GSSDDTAANR WAIGEGSSLG
     VIRSMKDPGK YGEPAIYKGS NWKPTATNPN DNNDQGGVHS NSGVGNKLAF LITDGQTFNG
     QTVTGIGIAK AAQLYWAAQR QLTANATYSS LGKALNSACS ANVSNNVAGT TAANCTQVAN
     AIKAVGIK