ID   DAP_BRUO2               Reviewed;         518 AA.
AC   A5VVL2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=BOV_A0889;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(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; CP000709; ABQ62502.1; -; Genomic_DNA.
DR   RefSeq; WP_006016489.1; NC_009504.1.
DR   AlphaFoldDB; A5VVL2; -.
DR   SMR; A5VVL2; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; ABQ62502; ABQ62502; BOV_A0889.
DR   GeneID; 45126255; -.
DR   KEGG; bov:BOV_A0889; -.
DR   HOGENOM; CLU_020027_0_4_5; -.
DR   OMA; VHPWADV; -.
DR   PhylomeDB; A5VVL2; -.
DR   Proteomes; UP000006383; Chromosome II.
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..518
FT                   /note="D-aminopeptidase"
FT                   /id="PRO_1000070873"
FT   REGION          477..487
FT                   /note="Important for specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        65
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   BINDING         481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
SQ   SEQUENCE   518 AA;  56782 MW;  130DC5EF02AA9CC4 CRC64;
     MPNIDLPTLE AFVHAIPQNY KGPGGAVAVV RNGEIVLRHA WGFADLAARK AMTPETRMPI
     CSVSKQFTCA VLLDCIGEPE MLDSALAAYL DQFGDGRPAV RDLCNNQSGL RDYWALTVLC
     GAAPEGIFLP DQAQNLLRRL KTTHFAPGTH YSYCNGNFRI LADLIEQHTG RSLADLLAER
     IFAPAAMKTA ELIPDTALFN ECTGYEGDTV HGFLPAINRI HWLGDAGICA SLDDMIAWEQ
     FIDRTRHDEN GLYRRLSSPQ TFADGAPAPY GFGLKFEETG GKRLTGHGGA LRGWRCQRWH
     CADERISTIV MFNFEGNASD AALKMMNAAL GIPPAKPVRA QANPGWFGSW LNPETGLVLS
     LEDAGGGRMK ARFGTGPEIM DISGENEAQS SMTTLRRDGD MIHLARKDEN LHLAMHRLKG
     EARQDIAGRY RSDELEADLL LVSEGGAIYG AFEGFLGKSD MYPLYAAGPD VWLLPVQRSM
     DAPSPGEWKL VFHRDAAGRI TGVTVGCWLA RGVEYKRL