ID   B4SS63_STRM5            Unreviewed;       654 AA.
AC   B4SS63;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ACF52695.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ACF52695.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_2996 {ECO:0000313|EMBL:ACF52695.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF52695.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF52695.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF52695.1,
RC   ECO:0000313|Proteomes:UP000001867};
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.
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DR   EMBL; CP001111; ACF52695.1; -; Genomic_DNA.
DR   RefSeq; WP_012511821.1; NC_011071.1.
DR   AlphaFoldDB; B4SS63; -.
DR   STRING; 391008.Smal_2996; -.
DR   KEGG; smt:Smal_2996; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ACF52695.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ACF52695.1};
KW   Protease {ECO:0000313|EMBL:ACF52695.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..654
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002826346"
SQ   SEQUENCE   654 AA;  72897 MW;  48A7DA9631F1FFDC CRC64;
     MKHRHLLLAS AIAAATLALA ACKKEAAPGT DTASSSAPAG ETADQFVARI NAEFKAAYPE
     MTSAQWLSST YINSDSERIA AKANERSLTQ LNSWIEQAAR FDGKPMSEDS KRAIHLLKLM
     SSMPAPRDPA KLAELTQIAT RMEGSYGAGK YCTDANDPNS CRQLGELEQV LARSRDYDKQ
     LDAWQGWHST TKSMRGDYQK FVGLVNEGAK GMGFTDAGQM WRSGYDMPPE QIGPETDRLW
     EQVKPMYEQL HCYARGKLDK TYGKDKAEVG NGLIAAHLLG NMWQQDWSNL WDQLEPYPGA
     GSLDITAALE KQYQTNLSAA LAKAGKDANV AAQYKAQREA ELRTAKQMTE RAQDFYVSLG
     MPSLPQSYWE KTQFIKPDDR DVVCHASAWD MNMEGDVRTK MCIKPNEENF TTIYHELGHI
     YYDLAYNPLP PLFQGGANDG FHEAIGDTIV LAMTPKYLSS IGLVDAPTES REAVINNQMR
     MALSGVSFLP FGLMIDRWRW GVFDGSITAD NYNKAWWDLK AKYQGVAPAS TRGEEFFDPG
     AKYHVPGNTP YTRYFLARIL QFQFYKGLCD ASGYKGPLHE CTFYGNKEAG QKYWAMLSKG
     ASQPWQATLK ELTGTDKLDA GPMIEYFSPV NEWLKQQNEG QMCGWQANAA PAAK
//