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Database: UniProt
Entry: A0A1C4S5M9_9ACTN
LinkDB: A0A1C4S5M9_9ACTN
Original site: A0A1C4S5M9_9ACTN 
ID   A0A1C4S5M9_9ACTN        Unreviewed;       277 AA.
AC   A0A1C4S5M9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=D-aminopeptidase DppA. Metallo peptidase. MEROPS family M55 {ECO:0000313|EMBL:SCE42303.1};
GN   ORFNames=GA0115242_136535 {ECO:0000313|EMBL:SCE42303.1};
OS   Streptomyces sp. SolWspMP-5a-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCE42303.1, ECO:0000313|Proteomes:UP000199131};
RN   [1] {ECO:0000313|EMBL:SCE42303.1, ECO:0000313|Proteomes:UP000199131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCE42303.1,
RC   ECO:0000313|Proteomes:UP000199131};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMCI01000323; SCE42303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4S5M9; -.
DR   OrthoDB; 9785420at2; -.
DR   Proteomes; UP000199131; 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; cd08663; DAP_dppA_1; 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:SCE42303.1};
KW   Hydrolase {ECO:0000313|EMBL:SCE42303.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015853-2};
KW   Protease {ECO:0000313|EMBL:SCE42303.1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR015853-2}.
FT   ACT_SITE        116
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   277 AA;  29513 MW;  C11960FA77B3A183 CRC64;
     MKILISADME GATGVTWPAD VLPGTPQWER CRSMFTSDVD AAVRGFFDGG ADEVLVNEAH
     WTMRNLLLEQ LDERAEMLTG RHKSLSMVEG VQHGDVDGIA FVGYHAGAGM EGVLAHTYLA
     NSITGVWVDG VRASEGLLNA RVVAEYGVPV VLVTGDDVAC EDALGYAPEA LKVAVKDHVS
     RYAAVCRTPA RTAADIRTAA AAAAKLAVRQ EPSQDGPFTI ALEFDAEHLA MAATVVPGVT
     RTGERRIAYT SPTMYEGIRT FKAVTTIASA AVEEQYG
//
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