ID   SHPI_STAHY              Reviewed;         438 AA.
AC   Q08002; Q09166;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Neutral metalloprotease ShpI {ECO:0000303|PubMed:8121397};
DE            EC=3.4.24.- {ECO:0000269|PubMed:8121397};
DE   Flags: Precursor;
GN   Name=shpI {ECO:0000303|PubMed:8121397};
OS   Staphylococcus hyicus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 93-115, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   COFACTOR, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 11249 / DSM 20459 / NCTC 10350 / 1;
RX   PubMed=8121397; DOI=10.1007/bf00281792;
RA   Ayora S., Goetz F.;
RT   "Genetic and biochemical properties of an extracellular neutral
RT   metalloprotease from Staphylococcus hyicus subsp. hyicus.";
RL   Mol. Gen. Genet. 242:421-430(1994).
CC   -!- FUNCTION: Protease that has a low substrate specificity. Catalyzes the
CC       hydrolysis of glucagon, melittin and oxidized beta-insulin at various
CC       positions in vitro. Is not able to cleave elastin or the synthetic
CC       substrates FAGLA (a substrate for neutral proteinases) and FALGPA (a
CC       substrate for collagenase). {ECO:0000269|PubMed:8121397}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:8121397};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- ACTIVITY REGULATION: Inhibited by metal- and zinc-specific inhibitors,
CC       such as EDTA and 1,10-phenanthroline in vitro. Is resistant to all
CC       inhibitors of serine, cysteine and aspartic proteases.
CC       {ECO:0000269|PubMed:8121397}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.4-8.5. {ECO:0000269|PubMed:8121397};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius. Unstable at temperatures
CC         above 45 degrees Celsius. {ECO:0000269|PubMed:8121397};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8121397}.
CC   -!- PTM: Several different N-terminal ends may be produced, the favored N-
CC       terminus is position 102.
CC   -!- SIMILARITY: Belongs to the peptidase M30 family. {ECO:0000305}.
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DR   EMBL; X73315; CAA51745.1; -; Genomic_DNA.
DR   PIR; S42581; S42581.
DR   RefSeq; WP_039646018.1; NZ_WMFP01000035.1.
DR   AlphaFoldDB; Q08002; -.
DR   STRING; 1284.SHYC_08015; -.
DR   MEROPS; M30.001; -.
DR   OMA; AHEYQHM; -.
DR   OrthoDB; 749253at2; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR019501; Peptidase_M30_hyicolysin.
DR   Pfam; PF10460; Peptidase_M30; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000305|PubMed:8121397"
FT   PROPEP          27..101
FT                   /evidence="ECO:0000269|PubMed:8121397"
FT                   /id="PRO_0000029231"
FT   CHAIN           102..438
FT                   /note="Neutral metalloprotease ShpI"
FT                   /id="PRO_0000029232"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT                   ECO:0000305|PubMed:8121397"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT                   ECO:0000305|PubMed:8121397"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT                   ECO:0000305|PubMed:8121397"
SQ   SEQUENCE   438 AA;  49693 MW;  368FAA36C5E84830 CRC64;
     MINKKKLVTS LVTSSLLATF TLGSFADAHT YIINNEDINK NAQESSIGTL KQNNFKQSTI
     DSMKPRNLQS FQEDKVFKAP KEKTPITERA RKSENALSNS KLNDVRSFTT VNMRTNENER
     TAAKLKYNGK NTNVWVADNY ITDKQAKNIG EEFDNKIDPL VKEKFGEPSD VDHDGKVNIL
     VYDIKDDFET TGSYTGGYFH PRDLYDVPHS NKAEVFYMDT YPSMGTDKNN LNEKKVYSTL
     AHEYQHMVNA NQKLLKEQKE DGMDVWLDEA FAMASEHMYL QKPLDHRIEY YNNSTSIANG
     HSLIKWNHRG DVLSNYALSY LFSQYLSAQS DNGDKIFKEI LQDPANTSEA LENAIHKHVD
     PKMSLGEFMT NFRVALEKKE ATGLHGFNGA PGLNSISPKP VRELPQTLAP QGSVMFETTS
     PIKVPKDKDE KVNYVKVK