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Protein

Murein tetrapeptide carboxypeptidase

Gene

ldcA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase.2 Publications

Catalytic activityi

GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanine + H2O = GlcNAc-MurNAc-L-alanyl-gamma-D-glutamyl-meso-diaminopimelate + D-alanine.1 Publication

Enzyme regulationi

Inhibited by beta-lactams containing a D-amino acid side chain.1 Publication

Pathwayi: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei106NucleophileBy similarity1
Active sitei200Charge relay systemBy similarity1
Active sitei270Charge relay systemBy similarity1

GO - Molecular functioni

  • carboxypeptidase activity Source: EcoCyc
  • serine-type peptidase activity Source: UniProtKB-KW

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • glycopeptide catabolic process Source: EcoCyc
  • peptidoglycan biosynthetic process Source: UniProtKB-KW
  • peptidoglycan turnover Source: EcoCyc
  • regulation of cell shape Source: UniProtKB-KW

Keywordsi

Molecular functionCarboxypeptidase, Hydrolase, Protease, Serine protease
Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEcoCyc:G6621-MONOMER
MetaCyc:G6621-MONOMER
UniPathwayiUPA00544

Protein family/group databases

MEROPSiS66.002

Names & Taxonomyi

Protein namesi
Recommended name:
Murein tetrapeptide carboxypeptidase (EC:3.4.17.13)
Alternative name(s):
LD-carboxypeptidase A
Muramoyltetrapeptide carboxypeptidase
Gene namesi
Name:ldcA
Synonyms:ycgQ
Ordered Locus Names:b1192, JW1181
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13898 ldcA

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Bacteriolysis during the stationary growth phase. Cells lacking this gene also accumulate UDP-MurNAc-tetrapeptide, an unusual compound that normally is not present at significant levels in E.coli cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001728371 – 304Murein tetrapeptide carboxypeptidaseAdd BLAST304

Proteomic databases

PaxDbiP76008
PRIDEiP76008

Interactioni

Protein-protein interaction databases

BioGridi4259643325 interactors.
DIPiDIP-10085N
IntActiP76008 4 interactors.
STRINGi316385.ECDH10B_1245

Structurei

3D structure databases

ProteinModelPortaliP76008
SMRiP76008
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S66 family.Curated

Phylogenomic databases

eggNOGiENOG4105EBE Bacteria
COG1619 LUCA
HOGENOMiHOG000025480
InParanoidiP76008
KOiK01297
OMAiMLTQWRL
PhylomeDBiP76008

Family and domain databases

Gene3Di3.40.50.107401 hit
3.50.30.601 hit
InterProiView protein in InterPro
IPR027461 Carboxypeptidase_A_C_sf
IPR029062 Class_I_gatase-like
IPR027478 LdcA_N
IPR003507 S66_fam
PANTHERiPTHR30237 PTHR30237, 1 hit
PfamiView protein in Pfam
PF02016 Peptidase_S66, 1 hit
PIRSFiPIRSF028757 LD-carboxypeptidase, 1 hit
SUPFAMiSSF141986 SSF141986, 1 hit
SSF52317 SSF52317, 1 hit

Sequencei

Sequence statusi: Complete.

P76008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFHLIAPS GYCIKQHAAL RGIQRLTDAG HQVNNVEVIA RRCERFAGTE
60 70 80 90 100
TERLEDLNSL ARLTTPNTIV LAVRGGYGAS RLLADIDWQA LVARQQHDPL
110 120 130 140 150
LICGHSDFTA IQCGLLAHGN VITFSGPMLV ANFGADELNA FTEHHFWLAL
160 170 180 190 200
RNETFTIEWQ GEGPTCRAEG TLWGGNLAML ISLIGTPWMP KIENGILVLE
210 220 230 240 250
DINEHPFRVE RMLLQLYHAG ILPRQKAIIL GSFSGSTPND YDAGYNLESV
260 270 280 290 300
YAFLRSRLSI PLITGLDFGH EQRTVTLPLG AHAILNNTRE GTQLTISGHP

VLKM
Length:304
Mass (Da):33,567
Last modified:February 1, 1997 - v1
Checksum:iBD801CA75E2AC25F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74276.1
AP009048 Genomic DNA Translation: BAA36050.1
PIRiE64865
RefSeqiNP_415710.1, NC_000913.3
WP_000051560.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74276; AAC74276; b1192
BAA36050; BAA36050; BAA36050
GeneIDi945756
KEGGiecj:JW1181
eco:b1192
PATRICifig|1411691.4.peg.1094

Similar proteinsi

Entry informationi

Entry nameiLDCA_ECOLI
AccessioniPrimary (citable) accession number: P76008
Secondary accession number(s): O87499
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 130 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome