ID   M5CKY0_STEMA            Unreviewed;       508 AA.
AC   M5CKY0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Putative exported protease {ECO:0000313|EMBL:CCP10746.1};
GN   ORFNames=SMSKK35_0616A {ECO:0000313|EMBL:CCP10746.1};
OS   Stenotrophomonas maltophilia SKK35.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=1118156 {ECO:0000313|EMBL:CCP10746.1, ECO:0000313|Proteomes:UP000012178};
RN   [1] {ECO:0000313|EMBL:CCP10746.1, ECO:0000313|Proteomes:UP000012178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKK35 {ECO:0000313|EMBL:CCP10746.1,
RC   ECO:0000313|Proteomes:UP000012178};
RA   Linke B., Adamek M., Schwartz T.;
RT   "Stenotrophomonas maltophilia SKK35 and RA8 genome sequencing: analysis and
RT   comparison of viurlence genes.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCP10746.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CALN01000488; CCP10746.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5CKY0; -.
DR   Proteomes; UP000012178; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   PANTHER; PTHR43798:SF27; HYDROLASE ALPHA_BETA HYDROLASE FOLD FAMILY; 1.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CCP10746.1};
KW   Protease {ECO:0000313|EMBL:CCP10746.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..508
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004064551"
FT   DOMAIN          98..462
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   508 AA;  54072 MW;  AA8E313EED978874 CRC64;
     MQRHHLALAG MLASLMLAGC SQPPSADTRG DSDAPSRRFG AIEFQPCTLS TEGASANVEA
     QCATLQVPED RAHPGGRQID LRIAWLESGS SGAGQPDPVF FLAGGPGQAA SEVAVIVDSA
     LRQVRKQRDV FLIDQRGTGG SNPLSCLGAD GKELQMDEDA APTEASLRDY AQRCAASLQG
     RADARFYTTA EAIADLDAVR QALGVDRLNL VGGSYGTRVA QRYAIAYPQH TRSLVIDGVV
     PNDLVVGGEF ARTFDNAISL QSAQCRKDAA CSKRFPVDTR EQLRAVAETL RRAPVTVDYR
     DPGTNAPRQD VLSPDSVVGL AFAFSYVPEY SSLLPLVLDE AAQGRYAPLA SLVRGATRSM
     DFQINRGMQW SVICSEDAPR FQAPAESDDA LFGAEAARAF FAACPVWPHQ PAPAALTAPL
     KSDLPVLLLS GELDPVTPPR YAEQVLKGLP NGRALVARGQ GHGTLNAGCM PRLLGQFIDT
     TDAKALDASC LDTLSYVPAF TSFNGWTP
//