ID DAP_BRUAN Reviewed; 520 AA. AC Q9ZBA9; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 82. DE RecName: Full=D-aminopeptidase; DE EC=3.4.11.19; GN Name=dap; OS Brucella anthropi (Ochrobactrum anthropi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=529; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-58; CYS-61; SER-62; RP LYS-65 AND CYS-69, AND ACTIVITY REGULATION. RC STRAIN=ATCC 49237 / SCRC C1-38; RX PubMed=1540587; DOI=10.1021/bi00123a016; RA Asano Y., Kato Y., Yamada A., Kondo K.; RT "Structural similarity of D-aminopeptidase carboxypeptidase DD and beta- RT lactamases."; RL Biochemistry 31:2316-2328(1992). RN [2] RP PROTEIN SEQUENCE OF 2-26, SUBUNIT, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 49237 / SCRC C1-38; RX PubMed=2760064; DOI=10.1016/s0021-9258(18)71668-2; RA Asano Y., Nakazawa A., Kato Y., Kondo K.; RT "Properties of a novel D-stereospecific aminopeptidase from Ochrobactrum RT anthropi."; RL J. Biol. Chem. 264:14233-14239(1989). RN [3] RP CATALYTIC ACTIVITY. RX PubMed=16131658; DOI=10.1110/ps.051475305; RA Delmarcelle M., Boursoit M.-C., Filee P., Baurin S.L., Frere J.-M., RA Joris B.; RT "Specificity inversion of Ochrobactrum anthropi D-aminopeptidase to a D,D- RT carboxypeptidase with new penicillin binding activity by directed RT mutagenesis."; RL Protein Sci. 14:2296-2303(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-520, AND PROBABLE ACTIVE SITE. RX PubMed=10986464; DOI=10.1016/s0969-2126(00)00188-x; RA Bompard-Gilles C., Remaut H., Villeret V., Prange T., Fanuel L., RA Delmarcelle M., Joris B., Frere J.-M., Van Beeumen J.; RT "Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new RT member of the 'penicillin-recognizing enzyme' family."; RL Structure 8:971-980(2000). CC -!- FUNCTION: Hydrolyzes N-terminal residues in D-amino acid-containing CC peptides. 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:0000269|PubMed:16131658, CC ECO:0000269|PubMed:2760064}; 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. CC {ECO:0000269|PubMed:1540587}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=281 nm {ECO:0000269|PubMed:2760064}; CC Kinetic parameters: CC KM=0.65 mM for D-alanine amide (at 30 degrees Celsius) CC {ECO:0000269|PubMed:2760064}; CC pH dependence: CC Optimum pH is 8.5. {ECO:0000269|PubMed:2760064}; CC Temperature dependence: CC Optimum temperature is 45 degrees Celsius. CC {ECO:0000269|PubMed:2760064}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2760064}. CC -!- SIMILARITY: Belongs to the peptidase S12 family. {ECO:0000305}. 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; M84523; AAA25519.1; -; Genomic_DNA. DR PIR; A42209; A42209. DR PDB; 1EI5; X-ray; 1.90 A; A=1-520. DR PDBsum; 1EI5; -. DR AlphaFoldDB; Q9ZBA9; -. DR SMR; Q9ZBA9; -. DR MEROPS; S12.002; -. DR SABIO-RK; Q9ZBA9; -. DR EvolutionaryTrace; Q9ZBA9; -. 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; DD-peptidase/beta-lactamase superfamily; 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 PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1. DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1. DR Pfam; PF00144; Beta-lactamase; 1. DR Pfam; PF07930; DAP_B; 1. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR SUPFAM; SSF50886; D-aminopeptidase, middle and C-terminal domains; 2. PE 1: Evidence at protein level; KW 3D-structure; Aminopeptidase; Direct protein sequencing; Hydrolase; KW Protease. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2760064" FT CHAIN 2..520 FT /note="D-aminopeptidase" FT /id="PRO_0000250696" FT REGION 477..487 FT /note="Important for specificity" FT ACT_SITE 62 FT /note="Nucleophile" FT /evidence="ECO:0000305" FT ACT_SITE 65 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305" FT BINDING 481 FT /ligand="substrate" FT MUTAGEN 58 FT /note="M->F: No effect on enzymatic activity." FT /evidence="ECO:0000269|PubMed:1540587" FT MUTAGEN 61 FT /note="C->S: Alters sensitivity to FT p-chloromercuribenzoate." FT /evidence="ECO:0000269|PubMed:1540587" FT MUTAGEN 62 FT /note="S->G: Abolishes enzymatic activity." FT /evidence="ECO:0000269|PubMed:1540587" FT MUTAGEN 65 FT /note="K->N: Abolishes enzymatic activity." FT /evidence="ECO:0000269|PubMed:1540587" FT MUTAGEN 69 FT /note="C->S: No effect on enzymatic activity." FT /evidence="ECO:0000269|PubMed:1540587" FT HELIX 7..14 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 22..31 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 34..45 FT /evidence="ECO:0007829|PDB:1EI5" FT TURN 46..49 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 61..63 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 64..75 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 83..89 FT /evidence="ECO:0007829|PDB:1EI5" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 100..104 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 113..119 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 130..138 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 155..169 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 173..180 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:1EI5" FT TURN 209..211 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 232..244 FT /evidence="ECO:0007829|PDB:1EI5" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 252..256 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 282..291 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 294..301 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 306..316 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 318..330 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 348..351 FT /evidence="ECO:0007829|PDB:1EI5" FT TURN 353..355 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 358..363 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 368..372 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 378..384 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 394..398 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 401..406 FT /evidence="ECO:0007829|PDB:1EI5" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 411..417 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 428..432 FT /evidence="ECO:0007829|PDB:1EI5" FT TURN 433..436 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 437..444 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 447..454 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 465..468 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 471..476 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 480..483 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 486..494 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 500..507 FT /evidence="ECO:0007829|PDB:1EI5" FT STRAND 510..517 FT /evidence="ECO:0007829|PDB:1EI5" SQ SEQUENCE 520 AA; 57392 MW; CB364A8061DFBF4A CRC64; MSKFDTSALE AFVRHIPQNY KGPGGVVAVV KDGEVVLQHA WGFADLRTRT PMTLDTRMPI CSVSKQFTCA VLLDAVGEPE LLDDALEAYL DKFEDERPAV RDLCNNQSGL RDYWALSVLC GADPEGVFLP AQAQSLLRRL KTTHFEPGSH YSYCNGNFRI LADLIEAHTG RTLVDILSER IFAPAGMKRA ELISDTALFD ECTGYEGDTV RGFLPATNRI QWMGDAGICA SLNDMIAWEQ FIDATRDDES GLYRRLSGPQ TFKDGVAAPY GFGLNLHETG GKRLTGHGGA LRGWRCQRWH CADERLSTIA MFNFEGGASE VAFKLMNIAL GVSSSEVSRV EADSAWFGSW LDDETGLVLS LEDAGHGRMK ARFGTSPEMM DVVSANEARS AVTTIRRDGE TIELVRASEN LRLSMKRVKG EAKHDIIGRY HSDELDADLL LVSEGGAIYG AFEGFLGKSD MYPLYSVGSD VWLLPVQRSM DAPSPGEWKL VFRRDDKGEI TGLSVGCWLA RGVEYRRVQP //