ID   ASPN_STRM5              Reviewed;         417 AA.
AC   B4SLL0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Peptidyl-Asp metalloendopeptidase {ECO:0000312|EMBL:ACF50520.1};
DE            EC=3.4.24.33;
DE   AltName: Full=Endopeptidase Asp-N {ECO:0000250|UniProtKB:Q9R4J4};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0815;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Metalloprotease, specifically cleaves on the N-terminal side
CC       of aspartyl, glutamyl and cysteic acid residues.
CC       {ECO:0000250|UniProtKB:Q9R4J4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid
CC         bonds.; EC=3.4.24.33; Evidence={ECO:0000250|UniProtKB:Q9R4J4};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O75173};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75173};
CC   -!- SIMILARITY: Belongs to the peptidase M72 family. {ECO:0000305}.
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DR   EMBL; CP001111; ACF50520.1; -; Genomic_DNA.
DR   RefSeq; WP_012510180.1; NC_011071.1.
DR   AlphaFoldDB; B4SLL0; -.
DR   SMR; B4SLL0; -.
DR   STRING; 391008.Smal_0815; -.
DR   EnsemblBacteria; ACF50520; ACF50520; Smal_0815.
DR   KEGG; smt:Smal_0815; -.
DR   eggNOG; COG3291; Bacteria.
DR   HOGENOM; CLU_658751_0_0_6; -.
DR   OMA; SKWRTIM; -.
DR   OrthoDB; 1291184at2; -.
DR   BioCyc; SMAL391008:SMAL_RS04155-MON; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Signal; Zinc.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..417
FT                   /note="Peptidyl-Asp metalloendopeptidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000389139"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000250|UniProtKB:O75173,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O75173,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O75173,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O75173,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   417 AA;  44067 MW;  D975E98EFDF3E4C5 CRC64;
     MLSRSIGKAA GGLVLGLSVA AAAHAAPLFE PVTVLSRAAA GSEPALGKLL ATPSTATVQE
     VRVDAAATAQ PQLEFELLGQ RVQAVRSKVE SLPDGGSIWY GQFRSPSDRL TAATSNGQDD
     PGNSVILVRS GNTVTGSIRK DGKLYRLRPL GNRHVLVEVD ESRMPADHPA DYNQLPKIPM
     GNNDRIGIAQ ASSGTPATIR VLVVATNAAV AAYGGNMQSL VQLAVAESNQ GYVNSNVGIT
     LQLAGYETTS YTESGNFTTD LTRFRNTSDG YMDSIHTSRN NTAADVGVLL INNTSYCGLA
     SGIGSTASTA FAAVYWDCAT GYYSFAHEIG HLQSARHDIA SDPSTSPYAY GHGYRYEPAS
     GSRWRTIMAY DCSAGCPRLN YWSNPNISYN GVPMGIASSA DNQRVLVNTK ATIAAFR