ID   DAP_GLUOX               Reviewed;         525 AA.
AC   Q5FRJ7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=GOX1238;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60999.1; -; Genomic_DNA.
DR   RefSeq; WP_011252791.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FRJ7; -.
DR   SMR; Q5FRJ7; -.
DR   STRING; 290633.GOX1238; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; AAW60999; AAW60999; GOX1238.
DR   KEGG; gox:GOX1238; -.
DR   eggNOG; COG1680; Bacteria.
DR   HOGENOM; CLU_020027_0_4_5; -.
DR   OMA; RDYWAMT; -.
DR   Proteomes; UP000006375; Chromosome.
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; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..525
FT                   /note="D-aminopeptidase"
FT                   /id="PRO_0000250695"
FT   REGION          485..495
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         489
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
SQ   SEQUENCE   525 AA;  57398 MW;  72FA67DFC9187ACB CRC64;
     MSDSFSARLE AAVSALPARF PGPGGAVAVL KDGEVLVRHG WGYANVERRI PFTPSTLFRM
     CSITKQFTCG TLLDLYDDPS ELDADVDARL PQLDEPSPGM LHLAHNQSGL RDYWAVAMLH
     GAPIEGYFGD REARRVIDGT RTLQFQPGTS YSYVNQNFRL ISDILQDRTG RSFAELLQTS
     IFNPVGMERA ILAAETRAMP DGTVGYEGSV ESGFRPAINN IWWTGDAGLG ASLDDMIAWE
     RFIDETRDAP DSLYRRLTVP VTFSDGQPAP YGFGLQRTKM FGRDVTMHGG ALRGWRSHRL
     HVASERLSVV VMFNHMSAAQ VASAQILAAA LGVPYEPERS TQQPTALYGT YLERETGLSA
     RIEPAPGGAK LRYLMVPELL EGISATRAEA GSVVVKAQET AEGAEAVMER PGENRTSILA
     RCDETPGEDI AELAGVYRCE ELDEAEVTIE LAGGVVYGGF SGILGDGRME MLQRLAKDVW
     VLPCPRALDH TAPGDWTLAF ERQGGSVTAV RVGCWLARDL MYQRV