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Database: UniProt
Entry: A0A0G9HC02_9GAMM
LinkDB: A0A0G9HC02_9GAMM
Original site: A0A0G9HC02_9GAMM 
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
//
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