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Database: UniProt
Entry: A0A380NLN9_9FIRM
LinkDB: A0A380NLN9_9FIRM
Original site: A0A380NLN9_9FIRM 
ID   A0A380NLN9_9FIRM        Unreviewed;       271 AA.
AC   A0A380NLN9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=D-aminopeptidase {ECO:0000313|EMBL:SUP43344.1};
DE            EC=3.4.11.- {ECO:0000313|EMBL:SUP43344.1};
GN   Name=dppA {ECO:0000313|EMBL:SUP43344.1};
GN   ORFNames=NCTC12020_01151 {ECO:0000313|EMBL:SUP43344.1};
OS   Veillonella criceti.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=103891 {ECO:0000313|EMBL:SUP43344.1, ECO:0000313|Proteomes:UP000255367};
RN   [1] {ECO:0000313|EMBL:SUP43344.1, ECO:0000313|Proteomes:UP000255367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12020 {ECO:0000313|EMBL:SUP43344.1,
RC   ECO:0000313|Proteomes:UP000255367};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UHIO01000001; SUP43344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A380NLN9; -.
DR   OrthoDB; 9785420at2; -.
DR   Proteomes; UP000255367; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08770; DAP_dppA_3; 1.
DR   Gene3D; 3.30.1360.130; Dipeptide transport protein; 1.
DR   Gene3D; 3.40.50.10780; Dipeptide transport protein; 1.
DR   InterPro; IPR027476; DppA_N.
DR   InterPro; IPR007035; Peptidase_M55.
DR   InterPro; IPR036177; Peptidase_M55_sf.
DR   Pfam; PF04951; Peptidase_M55; 1.
DR   PIRSF; PIRSF015853; Pep_DppA; 1.
DR   SUPFAM; SSF63992; Dipeptide transport protein; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:SUP43344.1};
KW   Hydrolase {ECO:0000313|EMBL:SUP43344.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015853-2};
KW   Protease {ECO:0000313|EMBL:SUP43344.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255367};
KW   Zinc {ECO:0000256|PIRSR:PIRSR015853-2}.
FT   ACT_SITE        117
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-1"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015853-2"
SQ   SEQUENCE   271 AA;  30468 MW;  B0F4F436D3AEFE25 CRC64;
     MKLFISADIE GCAGWAFREE GHVGEFGYDN LRRQMTREVR LACEVAHATG AKEIVVKDGH
     GGANNIDPLK MPHYVTLIRG KSGHPYNMMV GLDSSFDAVA YIGYHAASGD VGFSGSHTST
     GQSLYIRLNG AVLSECMLNS YTALSMGVPP IFLAGDRAIC EQATRFLPFI ETAETKHGVG
     GATYCESPVI VEERIKDRLS RAIRKWQEIY KKQSYKIQWP ESFTYEVTFK DWQRAYKMSF
     YPGMEQVDDF TIRLISKSWL DIITAHSFIV Y
//
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