DAP_BRUAN
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 03-AUG-2022, entry version 78.
DE RecName: Full=D-aminopeptidase;
DE EC=3.4.11.19;
GN Name=dap;
OS Brucella anthropi (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; 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; -; 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 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 p-
FT 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
