ID A0A1H7S1E0_9FIRM Unreviewed; 473 AA.
AC A0A1H7S1E0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SEL65417.1};
GN ORFNames=SAMN04487770_11461 {ECO:0000313|EMBL:SEL65417.1};
OS Butyrivibrio sp. ob235.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1761780 {ECO:0000313|EMBL:SEL65417.1, ECO:0000313|Proteomes:UP000199418};
RN [1] {ECO:0000313|EMBL:SEL65417.1, ECO:0000313|Proteomes:UP000199418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB235 {ECO:0000313|EMBL:SEL65417.1,
RC ECO:0000313|Proteomes:UP000199418};
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; FOBE01000014; SEL65417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7S1E0; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000199418; 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: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:SEL65417.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:SEL65417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199418};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 422..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..288
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 91
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 473 AA; 51724 MW; 5D0191C7B9FDE401 CRC64;
MNYKGFINKL NIIISMVLIS VLLTQTWSFC HAETDLEAAQ NARKELPIQS NDTPGWPAGP
QIGAEAAILM DANTGTILYA KNIHEELYPA STTKIMTCLL AVENAGLNDR VDFSYEAIHS
VPADGSKIGM DAGEYLSLEE CLYGIMVGSA NEVANAVAEH VSGSIDGFID LMNEKAASLG
CTNTHFSNTN GLQASDHYTS AYDLALISSE FFSNELLCRV GNTPRYHFEP SAGQPDDFYL
NNKHKLISGE MSYPGIIGGK TGYTDLARET LVTCAERGGM KLVCVVFMEE SPSQFTDTVT
LFDYGFNNFI TVNIKSEESG YIPRDNAFFS SGNDIFKAPT SVLEFGKSDY VILPVNSSLS
DATSTVSYDN EDGSSNVIAT INYSFNDVPI GSGHILVSQA SSSQAASEDR DIKTIYLNMK
QIITYFAFAG FSLILLIYIS SLISTYSFGG SREDRKRLNR RKREARKRSG PKL
//
