ID A0A0G9HC02_9GAMM Unreviewed; 731 AA.
AC A0A0G9HC02;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Dipeptidyl carboxypeptidase II {ECO:0000313|EMBL:APG04093.1};
GN ORFNames=BJI69_09425 {ECO:0000313|EMBL:APG04093.1};
OS Luteibacter rhizovicinus DSM 16549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG04093.1, ECO:0000313|Proteomes:UP000182987};
RN [1] {ECO:0000313|Proteomes:UP000182987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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}.
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DR EMBL; CP017480; APG04093.1; -; Genomic_DNA.
DR RefSeq; WP_046967925.1; NZ_JPLB01000035.1.
DR AlphaFoldDB; A0A0G9HC02; -.
DR STRING; 1440763.BJI69_09425; -.
DR KEGG; lrz:BJI69_09425; -.
DR PATRIC; fig|1440763.5.peg.2208; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000182987; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:APG04093.1};
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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..731
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014228075"
FT DOMAIN 282..729
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 731 AA; 80911 MW; 99E1E49B42CCE97B CRC64;
MLKVRSLVIA TSIALTAACS SSNDAEKSAA PAPASTAPAP AATTAASAAV PASHVNPLLT
PSELPFQAPP FDKIVDADFQ PAIEEGMKQQ LAEVEAIANA TDEPSFDNTI VALEKSGVLL
KRAENVFSAL TGANTNDTLQ KVDEDESPKL AAHSDAIYLN DKLFKRVEAL HDERDSLKLD
PESARLLQVT YDDFVHAGAK LSEADKTKLK DLNKEESTLS TKFTNVLLAA TKAGALVVDD
KKSLDGMSDA DVEAASAAAK DRKLDGKYVV TLQNTTQQPA LQGMNDRDTR EKLFKASFDR
AEHGDANDTR EIITRIAQVR ADRAKLLGFP NYAAWKLDDQ MAKTPAAAEK FMERLAPAAV
ARATAESKDI QQVIDQEKGG FQVQAWDWDH YAEKVRKAKY DLDEAQIKPY FELDNVLQNG
VFYAANQLYG LTFKERKDIP VYQPDVRVFE VFDKDGTSMA LFYCDYFKRD NKNGGAWMSN
FVDQSKLFGL KPVVYNVANF TKPAAGQPAL LSFDDVTTMF HEFGHALHGM FAATQYPSLS
GANTARDFVE FPSQFNEQWA SDPKVFANYA KHYQTGAPMP DELVAKIKKA KSFNQGYAMS
ELISAALLDM QWHMIAPGAP KQDVDAFEAN ALKKAGFTLA QVPPRYRSSY FQHIWGNGYA
AGYYAYLWTQ MLDSDAFEWF KEHGGLTREN GQIFRDKILS RGNTEELGKL YRDFRGKDPS
IEPMLKDRGL K
//