ID   DAP_CERS1               Reviewed;         516 AA.
AC   A3PRU3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Rsph17029_3981;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-2007) 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; CP000578; ABN79059.1; -; Genomic_DNA.
DR   RefSeq; WP_011842788.1; NC_009050.1.
DR   AlphaFoldDB; A3PRU3; -.
DR   SMR; A3PRU3; -.
DR   MEROPS; S12.002; -.
DR   EnsemblBacteria; ABN79059; ABN79059; Rsph17029_3981.
DR   GeneID; 57472624; -.
DR   KEGG; rsh:Rsph17029_3981; -.
DR   HOGENOM; CLU_020027_0_4_5; -.
DR   OMA; RDYWAMT; -.
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..516
FT                   /note="D-aminopeptidase"
FT                   /id="PRO_1000070875"
FT   REGION          476..486
FT                   /note="Important for specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        61
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   ACT_SITE        64
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
FT   BINDING         480
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01960"
SQ   SEQUENCE   516 AA;  55262 MW;  D0B0E806234D5D18 CRC64;
     MTLDLDALDR ALDALPNLFR GPGGVAGVVK DGQVVASRAW GYADLTRRRP METGTRLPIC
     SISKQFTCGV LLDTLGDTAA YDARVAEFLP QFEGPLPTLR QLCDNQSGLR DYWALTVLQG
     AEATQTFRRE DALPLIARMK TGHFPPGTAY SYCNCNFRIV SEILESETGR ALPDLYAERI
     FGPAGMRTAE LTSDTRHPAD EVVGYEGSDA VGFFPADNGI FWIGDAGISA SLQDMLAYES
     WIDATRDDEN SIYRRISVPP AYVCGTPASY GFGLSHETVA GLKVTGHGGA LRGFRAQRFH
     AADERLSVVV IFNHEASAHA AASSLLAAAL GHEAPKGAGP EGWAGQWLDP ESGLLLRVGE
     DAEGLTLRFA TGPDRLTVGE DGVPRGAGVS LAREGATLVM NRTSDNLTVR AEPLPVVAVA
     DAGEIAGRYH ARELEADLVI EARDGGAYAG FEGLLGAGPM ERLHPVGPDV WIVTTRRSMD
     APAPGDWTLQ VRREGGAVAG LRLGCWLARR IDYARV