ID   ASPN_STRMK              Reviewed;         417 AA.
AC   B2FQP3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Peptidyl-Asp metalloendopeptidase {ECO:0000250|UniProtKB:Q9R4J4};
DE            EC=3.4.24.33;
DE   AltName: Full=Endopeptidase Asp-N {ECO:0000250|UniProtKB:Q9R4J4};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smlt0970;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1] {ECO:0000312|EMBL:CAQ44534.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ44534.1; -; Genomic_DNA.
DR   RefSeq; WP_012479256.1; NC_010943.1.
DR   AlphaFoldDB; B2FQP3; -.
DR   SMR; B2FQP3; -.
DR   STRING; 522373.Smlt0970; -.
DR   EnsemblBacteria; CAQ44534; CAQ44534; Smlt0970.
DR   KEGG; sml:Smlt0970; -.
DR   PATRIC; fig|522373.3.peg.936; -.
DR   eggNOG; COG3291; Bacteria.
DR   HOGENOM; CLU_658751_0_0_6; -.
DR   OMA; CMVARAD; -.
DR   OrthoDB; 1291184at2; -.
DR   Proteomes; UP000008840; 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; Reference proteome;
KW   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_5000342480"
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;  44141 MW;  9BAEEF497087578C CRC64;
     MLSRSIGKAA GGLVLGLSVA AAAHAAPLFE PVTVISRASA NSEPALGKLL ATPSTATVQE
     VRVDAAATAQ PQLEFELLGK RVQAVRSKVE ALPDGGSIWY GQFRSPSDRL TAATSSGQDD
     PGNSLILVRS GDTITGSIRK DGKLYRLRPL GNRHVLVEVD ESRMPADHPA DYNQLPKIPM
     ADNDHIGIAQ ASSGTPATIR VLVVATNAAV TAYGGNMQSL VQLAVAESNQ GYVNSNVGLT
     LQLAGYETTN YSESGNFTTD LSRFRGTSDG YMDSIHTSRN TTAADVGVLL INNSAYCGLA
     SGIGSTASTA FAAVYWDCAT GYYSFAHEIG HLQSARHDIA TDSSTSPYAY GHGYRYEPAT
     GTGWRTIMAY NCTRSCPRLN YWSNPNISYN GIPMGNASTA DNQRVLVNTK ATIAAFR