ID   A0A0R0BZQ3_9GAMM        Unreviewed;       721 AA.
AC   A0A0R0BZQ3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Dipeptidyl carboxypeptidase II {ECO:0000313|EMBL:KRG58216.1};
GN   ORFNames=ABB25_08015 {ECO:0000313|EMBL:KRG58216.1};
OS   Stenotrophomonas koreensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=266128 {ECO:0000313|EMBL:KRG58216.1, ECO:0000313|Proteomes:UP000051254};
RN   [1] {ECO:0000313|EMBL:KRG58216.1, ECO:0000313|Proteomes:UP000051254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17805 {ECO:0000313|EMBL:KRG58216.1,
RC   ECO:0000313|Proteomes:UP000051254};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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:KRG58216.1}.
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DR   EMBL; LDJH01000012; KRG58216.1; -; Genomic_DNA.
DR   RefSeq; WP_057665678.1; NZ_LDJH01000012.1.
DR   AlphaFoldDB; A0A0R0BZQ3; -.
DR   PATRIC; fig|266128.3.peg.475; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000051254; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KRG58216.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051254};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..721
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006393276"
FT   DOMAIN          261..713
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   721 AA;  78569 MW;  B7EEFCB9908D71E1 CRC64;
     MPTRLALALA LSLGLSAPAF ADAAPNAATA QAANPFFAES ALPLHYPAFD RIADSDFAPA
     FDAGMAQELE EVEAIANNPA AATFDNTILA MERSGAILQR ARTVFSALAG ADTNDARKAL
     QTQYATRFAA HRDAIALNSK LFERIAALYA QRNDLGLDAE GVRLIERYYE NFERGGARLS
     DADKAKVKAI NAELAELGAK FNLNVLNEVN SSYIVVEDVA ELAGLSEGQI AATAEAAKAR
     GLEGKYVIAL LNTTGQPLLS NLANRDLRQK LYEASINRGS KGGDYDNTAL VSRIMALRAE
     KAALMGHPNF AAYGLGNQTA KTPEAVNAML RQLAPAAVAN AQREAADLQA MIDAEQQAAG
     QPTFQLQPWD WAYYSEKVRQ AKYNFDESQL KPYFEITRVL EDGVFFAAEK EFGLSFKQRT
     DLPVYHPDVT VYDVFNADGS QLAIFLFDPY ARASKRGGAW MNAYVSQSGL TGDLPVVANH
     LNIPKPPVGQ PTLLTWDEVT TTFHEFGHAL HGMFSDVKYP SFAGTAVPRD FVEFPSQVNE
     MWADEPTILA NYAKHHQTGD AMPQALLDKV VAAAKFNQGF MTTEYLGAAM LDQAWHQISA
     GQVPAPADVI AFERKALEDA GIYYAPVPPR YRTTYFSHIM GGYSAGYYAY IWSEVLDANT
     QQWFKQNGGL TRANGDHFRK TLLSRGGSAD AMQIFRDFAG HEPQIGPLLE KRGLVPADAA
     Q
//