ID A0A1V4IVB7_9CLOT Unreviewed; 318 AA.
AC A0A1V4IVB7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase DacB {ECO:0000313|EMBL:OPJ63849.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:OPJ63849.1};
GN Name=dacB_1 {ECO:0000313|EMBL:OPJ63849.1};
GN ORFNames=CLORY_10330 {ECO:0000313|EMBL:OPJ63849.1};
OS Clostridium oryzae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1450648 {ECO:0000313|EMBL:OPJ63849.1, ECO:0000313|Proteomes:UP000190080};
RN [1] {ECO:0000313|EMBL:OPJ63849.1, ECO:0000313|Proteomes:UP000190080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28571 {ECO:0000313|EMBL:OPJ63849.1,
RC ECO:0000313|Proteomes:UP000190080};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium oryzae DSM 28571.";
RL Submitted (MAR-2017) 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:OPJ63849.1}.
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DR EMBL; MZGV01000007; OPJ63849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4IVB7; -.
DR STRING; 1450648.CLORY_10330; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000190080; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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-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:OPJ63849.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OPJ63849.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:OPJ63849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190080};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..295
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 92
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 152
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 318 AA; 35252 MW; 4CEA6B48EE096438 CRC64;
MRRVHRKKRK SPVSKLIIIF VLTIMIALVT GIGEKTYNFI KDSSTLINPM KLSGNSYFSD
IKLYSPHAIL VELNNRRTLM ECRSEERIYP ASLTKMMTAI VAIENVKNLR QPVTLPRGIF
HDLYTENASM AGFLPNEQVS AEDLLYGIML PSGADASIGL SIYTAGSETK FVEIMNSKAK
ELGMKHTHFT NVCGLQDANH YSTVKDLSVL LAYALKNSTF RRIFTSTKHY IPATNMHPSG
ITVYSTMFKS AGTGRFNGGR LLGGKTGYTE EAGLCLASLA EKNGKEYILV TAGAEGDHKT
KQYDILDALN VYGKIKKE
//
