DACD_SALTY
ID DACD_SALTY Reviewed; 390 AA.
AC P37604; P37605;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=D-alanyl-D-alanine carboxypeptidase DacD;
DE Short=DD-carboxypeptidase;
DE Short=DD-peptidase;
DE EC=3.4.16.4;
DE AltName: Full=Penicillin-binding protein 6B;
DE Short=PBP-6B;
DE Flags: Precursor;
GN Name=dacD; Synonyms=phsE, phsF; OrderedLocusNames=STM2062;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7737516; DOI=10.1016/0378-1119(94)00930-q;
RA Alami N., Hallenbeck P.C.;
RT "Cloning and characterization of a gene cluster, phsBCDEF, necessary for
RT the production of hydrogen sulfide from thiosulfate by Salmonella
RT typhimurium.";
RL Gene 156:53-57(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-255.
RC STRAIN=LT2;
RX PubMed=7751291; DOI=10.1128/jb.177.10.2813-2820.1995;
RA Heinzinger N.K., Fujimoto S.Y., Clark M.A., Moreno M.S., Barrett E.L.;
RT "Sequence analysis of the phs operon in Salmonella typhimurium and the
RT contribution of thiosulfate reduction to anaerobic energy metabolism.";
RL J. Bacteriol. 177:2813-2820(1995).
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: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}. Note=N-terminal lies in the periplasmic
CC space. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68435.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA68436.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L31538; AAA68435.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L31538; AAA68436.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20966.1; -; Genomic_DNA.
DR EMBL; L32188; AAC36937.1; -; Genomic_DNA.
DR PIR; D57143; D57143.
DR RefSeq; NP_461007.1; NC_003197.2.
DR RefSeq; WP_000925042.1; NC_003197.2.
DR AlphaFoldDB; P37604; -.
DR SMR; P37604; -.
DR STRING; 99287.STM2062; -.
DR MEROPS; S11.009; -.
DR PaxDb; P37604; -.
DR EnsemblBacteria; AAL20966; AAL20966; STM2062.
DR GeneID; 1253583; -.
DR KEGG; stm:STM2062; -.
DR PATRIC; fig|99287.12.peg.2184; -.
DR HOGENOM; CLU_027070_8_1_6; -.
DR OMA; IQAGSWV; -.
DR PhylomeDB; P37604; -.
DR BioCyc; SENT99287:STM2062-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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; 2.60.410.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR SUPFAM; SSF69189; SSF69189; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..390
FT /note="D-alanyl-D-alanine carboxypeptidase DacD"
FT /id="PRO_0000027235"
FT ACT_SITE 65
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 131
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 390 AA; 43097 MW; E7BD51C17CE8F01B CRC64;
MLLKRRLFIA ASLFAMHLSP ALAADAVSFA PQPPAIDAGA WVLMDYTTGQ VLTAGNEHQQ
RNPASLTKLM TGYVVDRAID SHRISPDDIV TVGRDAWAKD NPVFVGSSLM FLKEGDRVSV
RDLSRGLIVD SGNDACVALA DYIAGGQPQF VAMMNSYVKK LNLQDTHFET VHGLDAPGQH
SSAYDLAVLS RAIIHGEPEF YHMYSEKSLT WNGITQQNRN GLLWDKTMHI DGLKTGHTSG
AGFNLIASAV DGQRRLIAVV MGAKSSKGRE EQARKLLQWG QQNFATVQIL HSGKKVGSER
IWYGDKEKIA LGTEQDFWMA LPKAEIPHIK AKYVLDRKEL EAPIAAHQQV GEIELYDRDK
LIAQWPLVTL ESVGKGGMFS RLSDYFQHKA
