LDCA_ECO57
ID LDCA_ECO57 Reviewed; 304 AA.
AC Q8XDJ8;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=Z1955, ECs1688;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56043.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35110.1; -; Genomic_DNA.
DR PIR; G85697; G85697.
DR PIR; G90839; G90839.
DR RefSeq; NP_309714.1; NC_002695.1.
DR RefSeq; WP_000051572.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XDJ8; -.
DR SMR; Q8XDJ8; -.
DR STRING; 155864.EDL933_1887; -.
DR MEROPS; S66.002; -.
DR EnsemblBacteria; AAG56043; AAG56043; Z1955.
DR EnsemblBacteria; BAB35110; BAB35110; ECs_1688.
DR GeneID; 913181; -.
DR KEGG; ece:Z1955; -.
DR KEGG; ecs:ECs_1688; -.
DR PATRIC; fig|386585.9.peg.1785; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_0_1_6; -.
DR OMA; MLTQWRL; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome;
KW Serine protease.
FT CHAIN 1..304
FT /note="Murein tetrapeptide carboxypeptidase"
FT /id="PRO_0000172839"
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"
SQ SEQUENCE 304 AA; 33602 MW; 0D973E385CB756C4 CRC64;
MSLFHLIAPS GYCIKQHAAL RGIQRLTDAG HQVNNVEVIA RRCERFAGTE TERLEDLNSL
ARLTTPNTIV LAVRGGYGAS RLLADIDWQA LVARQQYDPL LICGHSDFTA IQCGLLAQGN
VITFSGPMLV ANFGADELNT FTEHHFWLAL RNETFTIEWQ GEGPTCRAEG TLWGGNLAML
ISLIGTPWMP KIENGILVLE DINEHPFRVE RMLLQLYHAG ILPRQKAIIL GSFSGSTPND
YDAGYNLESV YAFLRSRLSI PLITGLDFGH EQRTVTLPLG AHAILTNTRE GTQLTISGHP
VLKM
