ID F8FQU5_PAEMK Unreviewed; 434 AA.
AC F8FQU5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 OrderedLocusNames=KNP414_00013 {ECO:0000313|EMBL:AEI38666.1},
GN KNP414_00679 {ECO:0000313|EMBL:AEI39275.1}, KNP414_06899
GN {ECO:0000313|EMBL:AEI45414.1};
OS Paenibacillus mucilaginosus (strain KNP414).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI39275.1, ECO:0000313|Proteomes:UP000006620};
RN [1] {ECO:0000313|Proteomes:UP000006620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620};
RA Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI39275.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KNP414 {ECO:0000313|EMBL:AEI39275.1};
RA Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AEI39275.1, ECO:0000313|Proteomes:UP000006620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNP414 {ECO:0000313|EMBL:AEI39275.1,
RC ECO:0000313|Proteomes:UP000006620};
RX PubMed=24158556;
RA Lu J.J., Wang J.F., Hu X.F.;
RT "Genome Sequence of Growth-Improving Paenibacillus mucilaginosus Strain
RT KNP414.";
RL Genome Announc. 1:e00881-13(2013).
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; CP002869; AEI38666.1; -; Genomic_DNA.
DR EMBL; CP002869; AEI39275.1; -; Genomic_DNA.
DR EMBL; CP002869; AEI45414.1; -; Genomic_DNA.
DR RefSeq; WP_013913832.1; NC_015690.1.
DR AlphaFoldDB; F8FQU5; -.
DR MEROPS; S11.001; -.
DR KEGG; pms:KNP414_00013; -.
DR KEGG; pms:KNP414_00679; -.
DR KEGG; pms:KNP414_06899; -.
DR PATRIC; fig|1036673.3.peg.11; -.
DR HOGENOM; CLU_027070_8_2_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006620; 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-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:AEI39275.1}; 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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..434
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038328810"
FT DOMAIN 313..409
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 74
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 434 AA; 47385 MW; 9028E60D0A1F51FB CRC64;
MFVRAKRICS TLAVTLLLHT TLAAVQPAAV RAEEAPPAQS TELQLNAKSA VLMDAATGQI
LYQYNADVAY PPASMAKMMT EYLVMEAVDQ GKLKLDEMVT TSQYAADVIG SGQLLAANEQ
ATVDNLFAAM SIYSSNDASV ALAERIAGTE EKFAQMMNDK AKEFGLSPQA HFNNATGLSI
ADLGKYAPKE NKQETMLTAK DAAIIAYHMI KDHKKVLEYT KTSSRKFREK DAAPMVNWNW
MLEANKDNAN FKRYAYTGLD GLKTGHTDEA GYCFTGTAER NGMRLISVVM GTPTEPKRFE
ETRKVLDYGF NNFESKQIAA AGAPISSMQT VNIKKGVETE VPVVTEQEMK LVVKKGTPDD
QIQVTGQAVA DEAKLTAPIQ KGQVVGTAKV TYNGSEHTVN LVAAQDVEKG SWIRLFFRAI
KNFFVDTING AKKG
//
