ID   DAP_BRUA4               Reviewed;         520 AA.
AC   A6WYS5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Oant_1412;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(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; CP000758; ABS14129.1; -; Genomic_DNA.
DR   RefSeq; WP_012091479.1; NC_009667.1.
DR   AlphaFoldDB; A6WYS5; -.
DR   SMR; A6WYS5; -.
DR   STRING; 439375.Oant_1412; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; ABS14129; ABS14129; Oant_1412.
DR   KEGG; oan:Oant_1412; -.
DR   PATRIC; fig|439375.7.peg.1481; -.
DR   eggNOG; COG1680; Bacteria.
DR   HOGENOM; CLU_020027_0_4_5; -.
DR   OMA; VHPWADV; -.
DR   OrthoDB; 537440at2; -.
DR   PhylomeDB; A6WYS5; -.
DR   Proteomes; UP000002301; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..520
FT                   /note="D-aminopeptidase"
FT                   /id="PRO_1000070874"
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   520 AA;  57486 MW;  C06D71D028098EED CRC64;
     MSKFDLSALE TFVRTIPQHY KGPGGAVAVL KDGKVVLRHA WGFADLSTRK AMTPETRMPI
     CSVSKQFTCA VLLDSVGEPE VLDDALAAYL DKFAEKRPSV RDLCNNQSGL RDYWALTVLC
     GADPEGVFLP EQAQSLLRRL KTTHFAPGTH YSYCNGNFRI LADLIEQHTG RSLIELLSER
     IFQPAGMKTA ELIPDTALFD ECTGYEGDTV RGFLPAVNRI HWMGDAGICA SLDDMIAWEQ
     FIDATRDDES GIYRRLSGLQ TFSDGAAAPY GLGLKFEETG GKRLTGHGGA LRGWRCQRWH
     CADERLSTIA MFNFEGGASD VAFKLMNIAL GVPTSEQVRV AADAVWFGSW LDHETGLVLS
     LEDAGRGRMK ARFGTGPEMM DVVGENEARS SMTAIRRDGD TIHLAREDEN LSLTMQRLKG
     AAKQDIAGHY RSDELEADLL IVDEGGAFYG AFEGFLGKSD MYSLYEAGPD VWLLPVQRSM
     DAPSPGEWKL VFHRDAKGEI TGMTVGCWLA RHVDYRRIQE