ID A0A1T5DK02_9FIRM Unreviewed; 342 AA.
AC A0A1T5DK02;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SKB71820.1};
GN ORFNames=SAMN06296386_104155 {ECO:0000313|EMBL:SKB71820.1};
OS Lachnospiraceae bacterium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1898203 {ECO:0000313|EMBL:SKB71820.1, ECO:0000313|Proteomes:UP000191179};
RN [1] {ECO:0000313|EMBL:SKB71820.1, ECO:0000313|Proteomes:UP000191179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1P17 {ECO:0000313|EMBL:SKB71820.1,
RC ECO:0000313|Proteomes:UP000191179};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; FUZG01000004; SKB71820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5DK02; -.
DR Proteomes; UP000191179; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
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; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:SKB71820.1};
KW 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:0000313|EMBL:SKB71820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191179};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 93..322
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 119
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 176
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 342 AA; 36710 MW; 5126B53DD4CD41B2 CRC64;
MNGVRCINNM SLYNLIRRPA AMAGLFLASV MLFTSCGSKS YSVPFDVNTT KSAFRFETNN
SRSIASSFAE NLAVVSGDMT PGEEISFGEN SYGSAILVNV DKHEVMYSRN ATAQLYPASM
TKVLTAVVAL ENASLDTVLT ANDNCVFTAG DVQKIGLKPG DTMTLDQALH LLLIYSANDV
AALIAENIGG SIEGFSTMMN AKARELGATN SNFVNPHGLH DEQHYTTAYD MYLIFNEAIK
DDTITQIIGM NSYTTSYKNS AGEEVTFSCD TTNRYLKGLV TSPSNVTVVG GKTGTTIAAG
ACLVQLSRDS AGRNYITCVM KGNNIDVTYS KTNSLLSMID SN
//
