ID   G7UR54_PSEUP            Unreviewed;       693 AA.
AC   G7UR54;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Dipeptidyl carboxypeptidase {ECO:0000313|EMBL:AER55865.1};
GN   OrderedLocusNames=DSC_06070 {ECO:0000313|EMBL:AER55865.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER55865.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER55865.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER55865.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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DR   EMBL; CP003093; AER55865.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7UR54; -.
DR   STRING; 1045855.DSC_06070; -.
DR   KEGG; psd:DSC_06070; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000005870; 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; -; 1.
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; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:AER55865.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:AER55865.1};
KW   Protease {ECO:0000313|EMBL:AER55865.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..693
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003504251"
SQ   SEQUENCE   693 AA;  76831 MW;  3D5C1C4F72E88B18 CRC64;
     MKPRHLVFAT AACLSLAGLS GCGSDQPATP DGVPPAPKGE TAEEFVERIN TGLRAQSPEL
     NAAQWLSSTY INDDSQRVAS RANERALTQL NAWITQSRRF EGKQMPPQTA RAIQLLRLMT
     AMPAPQDPQK LAELTRIATQ MEGMYGAGTY CTGEGQARSC RQLGALESVL ASSRDYDAQL
     DAWQGWHSIA PPMRERYTRF VALVNEGAQD MGFADAGELW RSGYDMAPGE VAAETNRLWS
     QVKPLYEQLH CYARGKLEAH YGMRGQVDGG LLPAHLLGNM WQQDWSNLWD LLQPYPEAGS
     LDITGALQAL DDAQYEKTLK TAALAPEDPF EGARDAAYTA QLQALGHDPD DAERTRLNRL
     AYDQAIARVA DLRRAAALAG AKAMAARAQD FYTSLGMPSL PKSYWQKSQF IKPRDREVVC
     HASAWDMDMT GDVRTKMCIE PDEESFTTLY HELGHLYYDL AYNSQPPVFQ GGANDGFHEA
     IGDTIVLAMT PRYLASIGLV KDAPTGEQAL VNAQMRMALS KVAFLPFGLM IDRWRWGVFD
     GSITPEHYNS AWWQLKAQYQ GVAPATPRGE EYFDAGAKYH VPGNTPYTRY FMAHILQFQF
     YKALCDASGH TGPLNQCSFY GNKRAGQKFW AMLQKGSSQP WPDTLKGLTG SDRMDAAPML
     EYFQPLDAWL KQQNEGKTCG WSAPAASQRS PRP
//