ID A0A1I7FHF0_9FIRM Unreviewed; 321 AA.
AC A0A1I7FHF0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:SFU35574.1};
GN ORFNames=SAMN05216540_101247 {ECO:0000313|EMBL:SFU35574.1};
OS Butyrivibrio sp. M55.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1855323 {ECO:0000313|EMBL:SFU35574.1, ECO:0000313|Proteomes:UP000199511};
RN [1] {ECO:0000313|EMBL:SFU35574.1, ECO:0000313|Proteomes:UP000199511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M55 {ECO:0000313|EMBL:SFU35574.1,
RC ECO:0000313|Proteomes:UP000199511};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPCD01000001; SFU35574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7FHF0; -.
DR Proteomes; UP000199511; 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:SFU35574.1};
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:SFU35574.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199511};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..321
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038609510"
FT DOMAIN 72..302
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 97
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 321 AA; 34835 MW; 36C6BEE6B95F8CEF CRC64;
MKCISKPCSF FVIMLMLSSV YLSGCSSIPY EAKYSIDKAT SSNRCEPFAA DKCVADVEDI
TSQDMQVNDK VSAGLFDINR RRTLYAKNVH ERLKPASLTK VMTAYIALKY YGDQLDKVLV
ADSSVYANES GAQALGLKEG CSMTLNEALH ALLIYSANDV ANLIATNLAG SIEGFADMMN
AEAMKLGATQ SNFKNPNGLN VEDHLVTAYD MYLIFSAAMK YDTFSEIISM NSYDVKWTDE
NGEGQSRTID NTNGYLRGDV AAPSGVTVIG GKTGTTNAAG HCLILLAKDG DGNPYIAVIM
RDTDGDTLYS DMTNMLNEIV K
//
