GenomeNet

Database: UniProt
Entry: A0A1M4N5G5_9CLOT
LinkDB: A0A1M4N5G5_9CLOT
Original site: A0A1M4N5G5_9CLOT 
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
//
DBGET integrated database retrieval system