DACX_STRSK
ID DACX_STRSK Reviewed; 291 AA.
AC P39042;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=D-alanyl-D-alanine carboxypeptidase;
DE Short=DD-carboxypeptidase;
DE Short=DD-peptidase;
DE EC=3.4.16.4;
DE AltName: Full=Penicillin-binding protein;
DE Short=PBP;
DE Flags: Precursor;
OS Streptomyces sp. (strain K15).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1958;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1930140; DOI=10.1042/bj2790223;
RA Palomeque-Messia P., Englebert S., Leyh-Bouille M., Nguyen-Disteche M.,
RA Duez C., Houba S., Dideberg O., van Beeumen J., Ghuysen J.-M.;
RT "Amino acid sequence of the penicillin-binding protein/DD-peptidase of
RT Streptomyces K15. Predicted secondary structures of the low Mr penicillin-
RT binding proteins of class A.";
RL Biochem. J. 279:223-230(1991).
RN [2]
RP PROTEIN SEQUENCE OF 30-85, AND ACTIVE SITE.
RX PubMed=2764892; DOI=10.1042/bj2600601;
RA Leyh-Bouille M., van Beeumen J., Renier-Pirlot S., Joris B.,
RA Nguyen-Disteche M., Ghuysen J.-M.;
RT "The Streptomyces K15 DD-peptidase/penicillin-binding protein. Active site
RT and sequence of the N-terminal region.";
RL Biochem. J. 260:601-604(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-291.
RX PubMed=10419503; DOI=10.1074/jbc.274.31.21853;
RA Fonze E., Vermeire M., Nguyen-Disteche M., Brasseur R., Charlier P.;
RT "The crystal structure of a penicilloyl-serine transferase of intermediate
RT penicillin sensitivity. The DD-transpeptidase of streptomyces K15.";
RL J. Biol. Chem. 274:21853-21860(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 30-291 OF WILD-TYPE AND MUTANTS
RP HIS-67; ALA-125; ALA-127 AND ASN-127, MUTAGENESIS OF LYS-67; SER-125 AND
RP CYS-127, AND REACTION MECHANISM.
RX PubMed=12627955; DOI=10.1021/bi027256x;
RA Rhazi N., Charlier P., Dehareng D., Engher D., Vermeire M., Frere J.-M.,
RA Nguyen-Disteche M., Fonze E.;
RT "Catalytic mechanism of the Streptomyces K15 DD-transpeptidase/penicillin-
RT binding protein probed by site-directed mutagenesis and structural
RT analysis.";
RL Biochemistry 42:2895-2906(2003).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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DR EMBL; X59965; CAA42591.1; -; Genomic_DNA.
DR PIR; S17674; S17674.
DR PDB; 1ES2; X-ray; 1.55 A; A=30-291.
DR PDB; 1ES3; X-ray; 2.20 A; A=30-291.
DR PDB; 1ES4; X-ray; 1.90 A; A=30-291.
DR PDB; 1ES5; X-ray; 1.40 A; A=30-291.
DR PDB; 1ESI; X-ray; 1.80 A; A=30-291.
DR PDB; 1J9M; X-ray; 1.65 A; A=30-291.
DR PDB; 1SKF; X-ray; 2.00 A; A=30-291.
DR PDBsum; 1ES2; -.
DR PDBsum; 1ES3; -.
DR PDBsum; 1ES4; -.
DR PDBsum; 1ES5; -.
DR PDBsum; 1ESI; -.
DR PDBsum; 1J9M; -.
DR PDBsum; 1SKF; -.
DR AlphaFoldDB; P39042; -.
DR SMR; P39042; -.
DR MEROPS; S11.004; -.
DR BRENDA; 3.4.16.4; 1284.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P39042; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW Peptidoglycan synthesis; Protease; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2764892"
FT CHAIN 30..291
FT /note="D-alanyl-D-alanine carboxypeptidase"
FT /id="PRO_0000027236"
FT ACT_SITE 64
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000269|PubMed:2764892"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:2764892"
FT ACT_SITE 125
FT /evidence="ECO:0000269|PubMed:2764892"
FT BINDING 242
FT /ligand="substrate"
FT MUTAGEN 67
FT /note="K->H: Almost no activity."
FT /evidence="ECO:0000269|PubMed:12627955"
FT MUTAGEN 125
FT /note="S->A: Almost no activity."
FT /evidence="ECO:0000269|PubMed:12627955"
FT MUTAGEN 127
FT /note="C->A,N: 10% of wild-type catalytic efficiency for
FT aminolysis reaction, but increased catalytic efficiency for
FT hydrolysis reaction."
FT /evidence="ECO:0000269|PubMed:12627955"
FT CONFLICT 70
FT /note="T -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="D -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1ES5"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:1ES5"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:1ES5"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:1ES5"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:1ES5"
SQ SEQUENCE 291 AA; 30258 MW; F31039CC7DB0962B CRC64;
MRLRRAAATV ITTGALLAAG TLGATPATAV TKPTIAAVGG YAMNNGTGTT LYTKAADTRR
STGSTTKIMT AKVVLAQSNL NLDAKVTIQK AYSDYVVANK PSQAHLIVGD KVTVRQLLYG
LMLPSGCDAA YALADKYGSG SQAAARVKSF IGKMNTAATN LGLHNTHFDS FDGIGNGANY
STPRHLTKIA SSAMKNSTFR TVVKTKAYTA KTVTKTGSIR TMDTWKNTNG LLSSYSGAIG
VKTGSGPEAK YCLVFAATRG GKTVIGTVLA STSIPARESD ATKIMNYGFA L
