ID   DAP_BRUSU               Reviewed;         518 AA.
AC   Q8FV99; G0KDV6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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};
GN   OrderedLocusNames=BRA0947, BS1330_II0939;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014292; AAN34118.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM20394.1; -; Genomic_DNA.
DR   RefSeq; WP_002965700.1; NZ_KN046805.1.
DR   AlphaFoldDB; Q8FV99; -.
DR   SMR; Q8FV99; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; AEM20394; AEM20394; BS1330_II0939.
DR   GeneID; 45053942; -.
DR   GeneID; 55592577; -.
DR   KEGG; bms:BRA0947; -.
DR   KEGG; bsi:BS1330_II0939; -.
DR   PATRIC; fig|204722.21.peg.346; -.
DR   HOGENOM; CLU_020027_0_4_5; -.
DR   OMA; VHPWADV; -.
DR   PRO; PR:Q8FV99; -.
DR   Proteomes; UP000007104; 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_0000250694"
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;  56873 MW;  DDC2F6B87CA39EFD CRC64;
     MPNIDLPTLE AFVHAIPQNY KGPGGAVAVV RNGEIVLRHA WGFADLAARK AMTPETRMPI
     CSVSKQFTCA VLLDCIGEPE MLDSALAAYL DQFEDGRPAV RDLCNNQSGL RDYWALTVLC
     GAAPEGIFLP DQAQNLLRRL KTTHFAPGTH YSYCNGNFRI LADLIEQHTG RSLADLLAER
     IFAPAAMKTA ELIPDTALFN ECTGYEGDTV RGFLPAINRI 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