ID A0A024P197_9BACI Unreviewed; 364 AA.
AC A0A024P197;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase DacB {ECO:0000313|EMBL:CDQ21910.1};
GN Name=dacB_1 {ECO:0000313|EMBL:CDQ21910.1};
GN ORFNames=BN983_00105 {ECO:0000313|EMBL:CDQ21910.1};
OS Halobacillus karajensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=195088 {ECO:0000313|EMBL:CDQ21910.1, ECO:0000313|Proteomes:UP000028868};
RN [1] {ECO:0000313|EMBL:CDQ21910.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ21910.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ21910.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ21910.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Halobacillus karajensis HK-03.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDQ21910.1}.
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DR EMBL; CCDI010000001; CDQ21910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024P197; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000028868; 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:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 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:CDQ21910.1};
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:CDQ21910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028868};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 28..249
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 60
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 364 AA; 41091 MW; 459574D61563286C CRC64;
MRRLLFIFLA IPLILPLCEV DRVQANPNIK VSAERAVLMD AESGRVLFEK NAYDPTLIAS
TTKIMTAIIA IESGMMEEDV KVSKRAVYTE GSSIYLTENE KIPLKDLVYG LMLRSGNDSA
VAIAEHVGGS VEGFVHLMNE KAAWLGMNNS HFENPHGLDG ETHYSSAYDL GLLMAYSMKN
DTFREVTGSE LYRSENRDYS WRNKNKMLTQ YYEPTNGGKT GFTKAAGRTL VTSAEKDGME
LIAVTLRASD DWNDHKRMFE WGFNNFETVK LQSEGVVEAN GQTYYIPRDI YYPLTLSEKE
DLRAAFYRYD EKNNTTNLAG VTAFMVGQTP VLEAPVWNER PSQSFFSEVK NFLNRMMGGV
PWST
//
