ID A0A1X9MA02_9BACI Unreviewed; 398 AA.
AC A0A1X9MA02;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=dacB {ECO:0000313|EMBL:ARK30238.1};
GN ORFNames=BkAM31D_10575 {ECO:0000313|EMBL:ARK30238.1};
OS Halalkalibacter krulwichiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK30238.1, ECO:0000313|Proteomes:UP000193006};
RN [1] {ECO:0000313|EMBL:ARK30238.1, ECO:0000313|Proteomes:UP000193006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM31D {ECO:0000313|EMBL:ARK30238.1,
RC ECO:0000313|Proteomes:UP000193006};
RA Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP020814; ARK30238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9MA02; -.
DR STRING; 199441.BkAM31D_10575; -.
DR KEGG; bkw:BkAM31D_10575; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000193006; Chromosome.
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-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 2.30.140.30; -; 1.
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; IPR012907; Peptidase_S11_C.
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; PF07943; PBP5_C; 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:ARK30238.1};
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:ARK30238.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000193006};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..268
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 286..368
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07943"
FT ACT_SITE 77
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 80
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 398 AA; 44728 MW; 726835A690949650 CRC64;
MSHQDATLLR QDGDLNMGKK LALILLAFLL IVTAVPLYAA AEQRNFSVSA QAAVLIEQES
GRILYGKNQD TPLRIASITK IMTAVLAIES GKMDEMVKVS SNAEGTEGSS IYLRAGEKIK
LEDLVYGLML RSGNDSAVAI AEHVGGSLEG FVYMMNEKAQ ELGMSNTMFQ NPHGLDDHED
HFSTAYDMAL LTQYAMELEQ YQTISATKSH RVDGEQIRVW RNKNRLLTEL YKYSTGGKTG
YTKRAKRTLV STAEKNGTEL IAVTLNAPSD WHDHMNLFNW AFQSYSMETL VEEGVMKEIE
DAFYKDNVYA PYSFEFPLTN VEREALTKEI TLYKPPADKR SAEFIPPQPV GKVEIKINND
VIGQVPLLFD PPEVEEKRSF WKKFLDIFSF TIGVRSSD
//
