ID   LDCA_ECOL6              Reviewed;         304 AA.
AC   P59238;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JAN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Murein tetrapeptide carboxypeptidase;
DE            EC=3.4.17.13;
DE   AltName: Full=LD-carboxypeptidase A;
DE   AltName: Full=Muramoyltetrapeptide carboxypeptidase;
GN   Name=ldcA; OrderedLocusNames=c1641;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=9712795; DOI=10.1128/iai.66.9.4411-4417.1998;
RA   Guyer D.M., Kao J.-S., Mobley H.L.T.;
RT   "Genomic analysis of a pathogenicity island in uropathogenic Escherichia
RT   coli CFT073: distribution of homologous sequences among isolates from
RT   patients with pyelonephritis, cystitis, and catheter-associated bacteriuria
RT   and from fecal samples.";
RL   Infect. Immun. 66:4411-4417(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Releases the terminal D-alanine residue from the cytoplasmic
CC       tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. Can
CC       also cleave D-Ala from murein derivatives containing the tetrapeptide,
CC       i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-
CC       tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein
CC       sacculi or cross-linked muropeptides. The tripeptides produced by the
CC       LcdA reaction can then be reused as peptidoglycan building blocks; LcdA
CC       is thereby involved in murein recycling (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-
CC         glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-
CC         glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl;
CC         Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3.4.17.13;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
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DR   EMBL; AF081283; AAC61707.1; -; Genomic_DNA.
DR   EMBL; AE014075; AAN80106.1; -; Genomic_DNA.
DR   RefSeq; WP_000051575.1; NC_004431.1.
DR   AlphaFoldDB; P59238; -.
DR   SMR; P59238; -.
DR   STRING; 199310.c1641; -.
DR   MEROPS; S66.002; -.
DR   EnsemblBacteria; AAN80106; AAN80106; c1641.
DR   KEGG; ecc:c1641; -.
DR   eggNOG; COG1619; Bacteria.
DR   HOGENOM; CLU_034346_0_1_6; -.
DR   OMA; MLTQWRL; -.
DR   BioCyc; ECOL199310:C1641-MON; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; 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; 3.40.50.10740; -; 1.
DR   Gene3D; 3.50.30.60; -; 1.
DR   InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR027478; LdcA_N.
DR   InterPro; IPR040449; Peptidase_S66_N.
DR   InterPro; IPR040921; Peptidase_S66C.
DR   InterPro; IPR003507; S66_fam.
DR   PANTHER; PTHR30237; PTHR30237; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 1.
DR   PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR   SUPFAM; SSF141986; SSF141986; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW   Hydrolase; Peptidoglycan synthesis; Protease; Serine protease.
FT   CHAIN           1..304
FT                   /note="Murein tetrapeptide carboxypeptidase"
FT                   /id="PRO_0000172838"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        248
FT                   /note="E -> K (in Ref. 1; AAC61707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   304 AA;  33547 MW;  015D9AE536279ED4 CRC64;
     MSLFHLIAPS GYCIKQHAAL RGIQRLTDAG HQVNNVEVIA RRCERFAGTE TERLEDLNSL
     ARLTTPNTIV LSVRGGYGAS RLLADIDWQA LVARQQHDPL LICGHSDFTA IQCGLLAQGN
     VITFSGPMLV ANFGADELNA FTEHHFWLAL RNKTFTIEWQ GEGPTCQTEG TLWGGNLAML
     ISLIGTPWMP KIENGILVLE DINEHPFRVE RMLLQLYHAG ILPRQKAIIL GSFSGSTPND
     YDAGYNLESV YAFLRSRLSI PLITGLDFGH EQRTVTLPLG AHAILNNTQE GTQLTISGHP
     VLKM