ID   DAP_CERSK               Reviewed;         516 AA.
AC   B9KTA6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=D-aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01960};
DE            EC=3.4.11.19 {ECO:0000255|HAMAP-Rule:MF_01960};
GN   Name=dap {ECO:0000255|HAMAP-Rule:MF_01960}; OrderedLocusNames=RSKD131_3424;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
CC   -!- FUNCTION: Hydrolyzes N-terminal residues in D-amino acid-containing
CC       peptides. {ECO:0000255|HAMAP-Rule:MF_01960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal D-amino acid from a peptide, Xaa-|-
CC         Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid
CC         amides and methyl esters also are hydrolyzed, as is glycine amide.;
CC         EC=3.4.11.19; Evidence={ECO:0000255|HAMAP-Rule:MF_01960};
CC   -!- ACTIVITY REGULATION: Inhibited by beta-lactam compounds such as 6-
CC       aminopenicillic acid, 7-aminocephalosporanic acid, benzylpenicillin and
CC       ampicillin. Inhibited by p-chloromercuribenzoate. {ECO:0000255|HAMAP-
CC       Rule:MF_01960}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01960}.
CC   -!- SIMILARITY: Belongs to the peptidase S12 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01960}.
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DR   EMBL; CP001151; ACM03284.1; -; Genomic_DNA.
DR   RefSeq; WP_012641007.1; NC_011958.1.
DR   AlphaFoldDB; B9KTA6; -.
DR   SMR; B9KTA6; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; ACM03284; ACM03284; RSKD131_3424.
DR   GeneID; 67448757; -.
DR   KEGG; rsk:RSKD131_3424; -.
DR   HOGENOM; CLU_020027_0_4_5; -.
DR   OMA; RDYWAMT; -.
DR   Proteomes; UP000001597; Chromosome 2.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.50; -; 2.
DR   Gene3D; 3.40.710.10; -; 1.
DR   HAMAP; MF_01960; D_aminopeptidase; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR027279; D_amino_pept/lipop_sf.
DR   InterPro; IPR023645; DAP.
DR   InterPro; IPR012856; DAP_B_dom.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF07930; DAP_B; 1.
DR   SUPFAM; SSF50886; SSF50886; 2.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease.
FT   CHAIN           1..516
FT                   /note="D-aminopeptidase"
FT                   /id="PRO_1000189067"
FT   REGION          476..486
FT                   /note="Important for specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        61
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        64
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   BINDING         480
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
SQ   SEQUENCE   516 AA;  55542 MW;  C683D5585BADBC45 CRC64;
     MTLDLDALDR ALDALPNLFR GPGGVAGVVK DGQVVASRAW GYADLTRRRP METATRLPIC
     SISKQFTCGV LLDTLGDTAA YDARVAEFLP QFEGPLPTLR QLCDNQSGLR DYWALTVLQG
     AEATQTFRRE DALPLIARMK TGHFPPGTAY SYCNCNFRIV SEILESETGR ALPDLYAERI
     FGPAGMRTAE LTSDTRHPAD EVVGYEGSDA VGFFPADNGI FWIGDAGISA SLQDMLAYES
     WIDATRDDEN SIYRRISVPP AYVCGTPASY GFGLSHETVA GVKVTGHGGA LRGFRAQRFH
     AADERLSVMV IFNHEASAHA AASSLLAAAL GHEAPKGARP EGWAGQWLDP ESGLLLRVGE
     DAEGLTLRFA TGPDRLTLGE DGVPRGAGVS LARDGAMLVM NRTSDNLTVR AEPLPVVTVA
     DAGEIAGRYH ARELEADLVI EARDGGAYAG FEGLLGEGPM ERLHPVGPDV WIVTTRRSMD
     APAPGDWTLQ VRREGGAVTG LRLGCWLARR IDYARV