ID   SMP_SERME               Reviewed;         352 AA.
AC   Q06517;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Extracellular minor metalloprotease;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=smp;
OS   Serratia marcescens (strain ATCC 21074 / E-15).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia; unclassified Serratia.
OX   NCBI_TaxID=617;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 53-57.
RX   PubMed=8449415; DOI=10.1016/0378-1119(93)90748-r;
RA   Kwon Y.T., Lee H.H., Rho H.M.;
RT   "Cloning, sequencing, and expression of a minor protease-encoding gene from
RT   Serratia marcescens ATCC21074.";
RL   Gene 125:75-80(1993).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0.;
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; M59854; AAA26553.1; -; Genomic_DNA.
DR   PIR; JU0153; JU0153.
DR   AlphaFoldDB; Q06517; -.
DR   SMR; Q06517; -.
DR   MEROPS; M04.025; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR032475; Protealysin_N_PP.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   Pfam; PF16485; PLN_propep; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
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..?
FT   PROPEP          ?..52
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8449415"
FT                   /id="PRO_0000028624"
FT   CHAIN           53..352
FT                   /note="Extracellular minor metalloprotease"
FT                   /id="PRO_0000028625"
FT   REGION          41..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        262
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   352 AA;  38515 MW;  D101C956426B163C CRC64;
     MPAQRMRSVI PPYMLRALLT RYAPQRDCAL HTLNHVQSLL GNKPLRSPTE KNARAGERSA
     ISTTPERHPT ARQTGAQGGA AQQPRRAVDE AYDHLGVTYD FFWQAYRRNS VDNKGLPLVQ
     RALRQGLPEQ LSGTASRWCS ETATARSSTV SPSPSTLVGH ELTHGSDRER SRLIYYQQSG
     ALNESLSDVF GSLVKQFHLQ QTADKADWLI GAGLLAKGIK GKGLRSMSAP GTAYDDPLLG
     KDPQPASMKD YIQTKEDNGG VHLNSGIPNR AFYLAATVLG GFAGKKPVTS GMTRCATKRC
     RKTPTSDHLR PRHGETRAGL RTKRGDKVQQ AWASGWQWSN ETAADAQSGY GH