ID A5D2Y2_PELTS Unreviewed; 392 AA.
AC A5D2Y2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN Name=DacC {ECO:0000313|EMBL:BAF59404.1};
GN OrderedLocusNames=PTH_1223 {ECO:0000313|EMBL:BAF59404.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59404.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
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 Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; AP009389; BAF59404.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D2Y2; -.
DR STRING; 370438.PTH_1223; -.
DR MEROPS; S11.005; -.
DR KEGG; pth:PTH_1223; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_8_0_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006556; Chromosome.
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; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 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 PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 1.
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; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:BAF59404.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..392
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039199962"
FT DOMAIN 287..377
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 74
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 392 AA; 42420 MW; EBD95B54E4C6E07B CRC64;
MLCKRKVVGV LVFFAIVICS AGRAAWAAQE AARSPKGNVP AALETTAESA ILLEPATGKI
IYEKEPHKRL PMASVTKLMT LLLAVEAVDE GKFKLTDRVV ASENAWEMGG SQIYLEPGEE
MSLWDLLLAI GLQSANDASV AVAEHIAGSE EAFVQAMNEK ARSLGLNNTN FVNCHGLTAD
NHYTSAHDMA MILKEGLKSP LFRKISAMKE YELRGGAFKL WNTNKLLWWY DGADAGKTGW
TEAAKYCLAS SAERDGLRLI CVVLGTPEPQ SHFRESTKLF DYGFARYKAV NLAPAGEVAG
TVRVGKGKAG SVKALTAEKV AVVVPKGEDK GFESRVELPG YIEAPVQKGQ EIGSYVVTKK
GEEVLRVKLV AGEDVPKASA IEQIRKVIDS VY
//
