ID A0A090IU10_9BACI Unreviewed; 440 AA.
AC A0A090IU10;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN Name=dacA {ECO:0000313|EMBL:CED99888.1};
GN ORFNames=B4166_0003 {ECO:0000313|EMBL:KIO64329.1}, B4167_0080
GN {ECO:0000313|EMBL:KIO73659.1}, BT1A1_0013
GN {ECO:0000313|EMBL:CED99888.1};
OS Caldibacillus thermoamylovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CED99888.1, ECO:0000313|Proteomes:UP000040576};
RN [1] {ECO:0000313|EMBL:CED99888.1, ECO:0000313|Proteomes:UP000040576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg Daniel;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000032076, ECO:0000313|Proteomes:UP000032097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4166 {ECO:0000313|EMBL:KIO64329.1,
RC ECO:0000313|Proteomes:UP000032097}, and B4167
RC {ECO:0000313|EMBL:KIO73659.1, ECO:0000313|Proteomes:UP000032076};
RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., Wells-Bennik M.,
RA Kuipers O.P.;
RT "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains,
RT Isolated From Food Products.";
RL Submitted (JAN-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 -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CCRF01000001; CED99888.1; -; Genomic_DNA.
DR EMBL; JXLT01000092; KIO64329.1; -; Genomic_DNA.
DR EMBL; JXLU01000029; KIO73659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090IU10; -.
DR PATRIC; fig|35841.7.peg.644; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000032076; Unassembled WGS sequence.
DR Proteomes; UP000032097; Unassembled WGS sequence.
DR Proteomes; UP000040576; Unassembled WGS sequence.
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-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR012907; Peptidase_S11_C.
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; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SMART; SM00936; PBP5_C; 1.
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:CED99888.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CED99888.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000040576};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 302..410
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
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 132
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 440 AA; 48829 MW; DE31555F05DF2525 CRC64;
MFKKKKPIMI YMIISFLLMA MLPFGGKQVS AETDSLNLKG SAAILVDGNT GKVLYEKNAD
ELLGVASMSK MMTEYIVLEA IKEGKISWDQ KVTISKFIHD LSSPSLGVST VGLTEGETYT
VKELYESMAI HSANASTVAL AELVGGSEEN FVKLMNEKAK KLGLKDYYFV NSSGLNNADM
LGNHPEGTDA NDENKMSARA TAKLAYRLIN DFPEVLQIAS KPVLNFRGEE FKNFNWMLPG
LVYEYEGVDG LKTGSTAYAG YNFTATAERN GQRLISVIMK TGSQQERFEE TKKLLDYGFN
NFSKEQLFPK NHAVKGKTSL PVVKGKEDSV KIATKEPLSL VIKNGEKEQY KPKLVLDEKK
INKEGKLTAP VKKGEVVGYV TYQYSGDDSG FLYPDQTVKV DVVAKEKVEK ANWFVLMFRG
MGGFFGNLWD GITSKVSSWF
//
