ID B2BCX1_PAEPO Unreviewed; 417 AA.
AC B2BCX1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 03-MAY-2023, entry version 51.
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=dac {ECO:0000313|EMBL:ACB54658.1};
OS Paenibacillus polymyxa (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1406 {ECO:0000313|EMBL:ACB54658.1};
RN [1] {ECO:0000313|EMBL:ACB54658.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PKB1 {ECO:0000313|EMBL:ACB54658.1};
RX PubMed=17400768; DOI=10.1128/AEM.02662-06;
RA Li J., Beatty P.K., Shah S., Jensen S.E.;
RT "Use of PCR-targeted mutagenesis to disrupt production of fusaricidin-type
RT antifungal antibiotics in Paenibacillus polymyxa.";
RL Appl. Environ. Microbiol. 73:3480-3489(2007).
RN [2] {ECO:0000313|EMBL:ACB54658.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PKB1 {ECO:0000313|EMBL:ACB54658.1};
RX PubMed=18291316; DOI=10.1016/j.chembiol.2007.12.014;
RA Li J., Jensen S.E.;
RT "Nonribosomal biosynthesis of fusaricidins by Paenibacillus polymyxa PKB1
RT involves direct activation of a D-amino acid.";
RL Chem. Biol. 15:118-127(2008).
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; EF451155; ACB54658.1; -; Genomic_DNA.
DR AlphaFoldDB; B2BCX1; -.
DR MEROPS; S11.001; -.
DR UniPathway; UPA00219; -.
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:ACB54658.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 306..402
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 68
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 417 AA; 45086 MW; 86B575C454D5C1E6 CRC64;
MSALPVVGNF DPNVATFAAG AATQATNITG TGSINPPSLA LRSAILIEPS TGQVLLSMNP
DEPLPPASMT KMMTEYIVAE QVKQGKLKWT DKVTVNENAS KSIGSRIFLA QGDQHTVEEL
YIAMAVGSAN DATVALAERV SGTEQDFVKL MNETAQKMGM KNTYFINSTG LDRKDMPTGF
QPDTDRETVM TARDAATLAG YIIKDHPDYT RFTTIQSYKF RPTDKAPIIN YNWMLEENKN
ITNFRKFAYP GLDGMKTGHT NNAGNCFTGT AERNGMRLIS VVMGADSDAH RFTETAKVLN
YGFDNFEVKQ VVAPKTVVKG VENVPVTKGT ETEVPIVTKD AVSFIVPKGA SNPKVTFTTN
ITPASSLVAP LKQGAKVGTI TYTYKTDGVD KGQTKTGSGY YDGVRGRLVP NAFPGNR
//
