ID A0A1M4N5G5_9CLOT Unreviewed; 389 AA.
AC A0A1M4N5G5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=dacF {ECO:0000313|EMBL:SCN21397.1};
GN ORFNames=N3C_0174 {ECO:0000313|EMBL:SCN21397.1};
OS Clostridium sp. N3C.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1776758 {ECO:0000313|EMBL:SCN21397.1, ECO:0000313|Proteomes:UP000184869};
RN [1] {ECO:0000313|EMBL:SCN21397.1, ECO:0000313|Proteomes:UP000184869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N3C {ECO:0000313|EMBL:SCN21397.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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}.
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; FMJL01000002; SCN21397.1; -; Genomic_DNA.
DR RefSeq; WP_074364177.1; NZ_FMJL01000002.1.
DR AlphaFoldDB; A0A1M4N5G5; -.
DR STRING; 1776758.N3C_0174; -.
DR OrthoDB; 9791132at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000184869; 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:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 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:SCN21397.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SCN21397.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184869};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 280..369
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT ACT_SITE 64
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 389 AA; 43400 MW; 7ACCE301A08CA31B CRC64;
MKKKFINIVM FCLIITLFIS SFGIRVKAEG EGIKVEAKSA VLVEPNSGKI LYEYNSHEKF
APASVTKIMT MLLAMEAIDS GKIKMSDKVT VSENAKKMGG STMLLDTGEV RTVEELLKGI
AIASGNDAAV AMAEYLGGSE EAFVNMMNDK AKALGMKDTS FKNCTGLPEE NHYSSAYDIY
LMSRELLKHP AILKYTGTYM ETISEGRKTP IELVNHNKLV RFFKGCDGLK TGFTNEAKYC
ISATATRDGV RMLAVIMGAP TYKIRNRDAS MLLNYGFSKF ESKQIVKKDE ELEKVPLNKS
GDKFFIVKAS EDLTITLEKG SANNISKKVT IDNNKKEYKK GEIIGYCEYY NNGELIGKIK
VYCDRDAKKS SGFFENLEFN FKNLFKHSI
//