ID A0A0H4NYL1_9BACI Unreviewed; 431 AA.
AC A0A0H4NYL1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AKP45765.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:AKP45765.1};
GN ORFNames=BSM4216_0418 {ECO:0000313|EMBL:AKP45765.1};
OS Bacillus smithii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP45765.1, ECO:0000313|Proteomes:UP000036353};
RN [1] {ECO:0000313|EMBL:AKP45765.1, ECO:0000313|Proteomes:UP000036353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP45765.1,
RC ECO:0000313|Proteomes:UP000036353};
RA Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA van Kranenburg R.;
RT "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT 4216T.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP012024; AKP45765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4NYL1; -.
DR STRING; 1479.BSM4216_0418; -.
DR KEGG; bsm:BSM4216_0418; -.
DR eggNOG; COG1686; Bacteria.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000036353; Chromosome.
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; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF11; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACA; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:AKP45765.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AKP45765.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:AKP45765.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 31..286
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 67
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 431 AA; 47808 MW; 94717CC2B7670B6A CRC64;
MIRYVHMYLV AILLVAGISM SFPSGRHSKA EAASDMSVHA KAAILVDAKS GKILFGQNMD
ESLSVASMSK LMTQYLILEK IQKGDLKWDD VYHADATDQD LSTRPGLGNV PLYQGQSYTV
RDLYNAMTLV SANAASRALG RMAGKSDKHF VQMMNNKAKQ LGLKHSSFVN TSGLNNQDLA
PYQVKGTASD GENKMSARDL ALLAYHFIHS FPNEMDIEKK ELDQFPVTDS YSIPLRNKNQ
LLPNGKYPYK GAIGLKTGMN DAAGYGIVAL AKRGQRELIA VIIDAKNKKG KRSSKARYMQ
AQKLLDYGFT HWDYEKISPE KFLPTNQQKI PVENGTKEKA AITSKTTVTE LVPKNGHSIK
AKLTLMPKFL TDQKKLKSPI QKGTVIGKIT LRDGSYGYLT TKLEKKAQVK ATVKEEIQKE
NWFAALMDGI F
//
