ID   B2FQE3_STRMK            Unreviewed;       654 AA.
AC   B2FQE3;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Angiotensin-converting enzyme like peptidyl dipeptidase protein {ECO:0000313|EMBL:CAQ46992.1};
GN   OrderedLocusNames=Smlt3574 {ECO:0000313|EMBL:CAQ46992.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ46992.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ46992.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ46992.1,
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; CAQ46992.1; -; Genomic_DNA.
DR   RefSeq; WP_005410621.1; NC_010943.1.
DR   AlphaFoldDB; B2FQE3; -.
DR   SMR; B2FQE3; -.
DR   EnsemblBacteria; CAQ46992; CAQ46992; Smlt3574.
DR   GeneID; 61467059; -.
DR   KEGG; sml:Smlt3574; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   Proteomes; UP000008840; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008840};
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_5002776399"
SQ   SEQUENCE   654 AA;  72883 MW;  48A7D8B1C1DC0AD1 CRC64;
     MKHRHLLLAS AIAAATLALA ACKKEAAPGT DTASSSAPAG ETADQFVARI NAEFKAAYPE
     MTSAQWLSST YINSDSERIA AKANERSLTQ LNSWIEQAAK 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 GPMIEYFTPV NEWLKQQNEG QMCGWQANAA PAAK
//