ID   B2FUF3_STRMK            Unreviewed;       296 AA.
AC   B2FUF3;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Serine aminopeptidase S33 domain-containing protein {ECO:0000259|Pfam:PF12146};
GN   OrderedLocusNames=Smlt1420 {ECO:0000313|EMBL:CAQ44959.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ44959.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ44959.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ44959.1,
RC   ECO:0000313|Proteomes:UP000008840};
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).
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DR   EMBL; AM743169; CAQ44959.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2FUF3; -.
DR   SMR; B2FUF3; -.
DR   ESTHER; strmk-b2fuf3; CarbLipBact_2.
DR   EnsemblBacteria; CAQ44959; CAQ44959; Smlt1420.
DR   KEGG; sml:Smlt1420; -.
DR   eggNOG; COG1647; Bacteria.
DR   HOGENOM; CLU_076594_1_0_6; -.
DR   Proteomes; UP000008840; Chromosome.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012354; Esterase_lipase.
DR   InterPro; IPR022742; Hydrolase_4.
DR   PANTHER; PTHR11614:SF121; CARBOXYLESTERASE; 1.
DR   PANTHER; PTHR11614; PHOSPHOLIPASE-RELATED; 1.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   PIRSF; PIRSF017388; Esterase_lipase; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008840}.
FT   DOMAIN          34..269
FT                   /note="Serine aminopeptidase S33"
FT                   /evidence="ECO:0000259|Pfam:PF12146"
FT   ACT_SITE        108
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017388-1"
FT   ACT_SITE        234
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017388-1"
FT   ACT_SITE        263
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017388-1"
SQ   SEQUENCE   296 AA;  32531 MW;  BF07D18F7C9F8DE5 CRC64;
     MKIALAILPS PLPSRSRQVT ESHDFFLPGG PQGVLLVHGL TGTPAEMRML GKGLNNAGFT
     VHGVQLPGHC GTVDDLLATT WEQWYQGVED AAAALRGKVD QLFVGGLSMG AVLSLALAAR
     RPEWVSGVGV YGATFRYDGW NIPAVARFSF LLPWFKRFNI GRDRMFMEEP PYGLRDERLR
     AQVSAAMLSG DSAAAGLPGN PWHALAEMRA LSNWTRRHLH QVTAPCLVMH AREDDVASMG
     NAELVMSRVS GPKELVVLED SYHMITIDRE RRDVIRRSAR FFTEIGERTG VLKAVA
//