DAP_BRUMB
ID DAP_BRUMB Reviewed; 518 AA.
AC C0RM93;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=BMEA_B0933;
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457;
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001489; ACO02726.1; -; Genomic_DNA.
DR RefSeq; WP_004685968.1; NC_012442.1.
DR AlphaFoldDB; C0RM93; -.
DR SMR; C0RM93; -.
DR PRIDE; C0RM93; -.
DR EnsemblBacteria; ACO02726; ACO02726; BMEA_B0933.
DR KEGG; bmi:BMEA_B0933; -.
DR HOGENOM; CLU_020027_0_4_5; -.
DR OMA; VHPWADV; -.
DR Proteomes; UP000001748; 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_1000189066"
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; 56887 MW; EBC9EA71E2CB3C57 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
KARQDIAGRY RSDELEADLL LVSEGGAIYG AFEGFLGKSD MYPLYAAGPD VWLLPVQRSM
DAPSPGEWKL VFHRDAAGRI TGVTVGCWLA RGVEYKRL