ID   DAP_BRUME               Reviewed;         518 AA.
AC   Q8YD27;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=BMEII0350;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008918; AAL53592.1; -; Genomic_DNA.
DR   PIR; AE3553; AE3553.
DR   RefSeq; WP_004682345.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YD27; -.
DR   SMR; Q8YD27; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; AAL53592; AAL53592; BMEII0350.
DR   GeneID; 29596073; -.
DR   KEGG; bme:BMEII0350; -.
DR   PATRIC; fig|224914.52.peg.3029; -.
DR   eggNOG; COG1680; Bacteria.
DR   OMA; VHPWADV; -.
DR   PhylomeDB; Q8YD27; -.
DR   Proteomes; UP000000419; 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_0000250693"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  56888 MW;  DDC14059404114FD 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 ARFGTGPEKM DISGENEAQS SMTTLRRDGD MIHLARKDEN LHLAMHRLKG
     EARQDIAGRY RSDELEADLL LVSEGGAIYG AFEGFLGKSD MYPLYAAGPD VWLLPVQRSM
     DAPSPGEWKL VFHRDAAGRI TGVTVGCWLA RGVEYKRL