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Protein

Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase

Gene

mepS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds. Partially suppresses a prc disruption mutant.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.

Pathwayi: cell wall polysaccharide biosynthesis

This protein is involved in the pathway cell wall polysaccharide biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway cell wall polysaccharide biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941NucleophileCurated
Active sitei145 – 1451Proton acceptorCurated

GO - Molecular functioni

  • cysteine-type peptidase activity Source: UniProtKB-KW
  • endopeptidase activity Source: EcoCyc

GO - Biological processi

  • capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan metabolic process Source: EcoCyc
  • peptidoglycan turnover Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciEcoCyc:G7147-MONOMER.
ECOL316407:JW2163-MONOMER.
MetaCyc:G7147-MONOMER.
UniPathwayiUPA00963.

Protein family/group databases

MEROPSiC40.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase (EC:3.4.-.-, EC:3.4.17.13)
Alternative name(s):
Lipoprotein Spr
Murein hydrolase MepS
Gene namesi
Name:mepS
Synonyms:spr, yeiV
Ordered Locus Names:b2175, JW2163
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14076. mepS.

Subcellular locationi

  • Cell outer membrane Curated; Lipid-anchor PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Unable to grow on nutrient agar at 42 degrees Celsius. A triple mepS-mepH-mepM mutant is inviable, whereas a double mepS-mepM will grow on a nutrient-poor medium but not on a rich medium, suggesting the 3 endopeptidases are functionally redundant in vivo. Depletion experiments of the double or triple mutants lead to cell lysis, as well as significantly decreased incorporation of mDAP into peptidogylcan sacculi and increased amounts of the enzyme's substrate (Tetra-Tetra-anhydro muropeptide).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941C → A: Loss of DD-endopeptidase activity, no complementation of double mepS-mepM deletion mutants. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626PROSITE-ProRule annotationAdd
BLAST
Chaini27 – 188162Murein DD-endopeptidase MepS/Murein LD-carboxypeptidasePRO_0000019763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi27 – 271N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi27 – 271S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP0AFV4.
PRIDEiP0AFV4.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

BioGridi4261093. 195 interactions.
IntActiP0AFV4. 8 interactions.
STRINGi511145.b2175.

Structurei

Secondary structure

1
188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 7712Combined sources
Helixi94 – 10411Combined sources
Helixi114 – 1174Combined sources
Helixi118 – 1203Combined sources
Beta strandi121 – 1244Combined sources
Helixi126 – 1283Combined sources
Beta strandi133 – 1397Combined sources
Turni140 – 1423Combined sources
Beta strandi143 – 1519Combined sources
Beta strandi154 – 1596Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 1686Combined sources
Helixi172 – 1776Combined sources
Beta strandi178 – 1836Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1GNMR-A63-188[»]
ProteinModelPortaliP0AFV4.
SMRiP0AFV4. Positions 63-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFV4.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C40 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107TT5. Bacteria.
COG0791. LUCA.
HOGENOMiHOG000229978.
InParanoidiP0AFV4.
KOiK13694.
OMAiWASRYMG.
PhylomeDBiP0AFV4.

Family and domain databases

Gene3Di3.90.1720.10. 1 hit.
InterProiIPR000064. NLP_P60_dom.
[Graphical view]
PfamiPF00877. NLPC_P60. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AFV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKSQPILRY ILRGIPAIAV AVLLSACSAN NTAKNMHPET RAVGSETSSL
60 70 80 90 100
QASQDEFENL VRNVDVKSRI MDQYADWKGV RYRLGGSTKK GIDCSGFVQR
110 120 130 140 150
TFREQFGLEL PRSTYEQQEM GKSVSRSNLR TGDLVLFRAG STGRHVGIYI
160 170 180
GNNQFVHAST SSGVIISSMN EPYWKKRYNE ARRVLSRS
Length:188
Mass (Da):21,040
Last modified:December 20, 2005 - v1
Checksum:i65DCEEDBDDC76098
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86610 Genomic DNA. Translation: BAA13140.1.
U00096 Genomic DNA. Translation: AAC75236.1.
AP009048 Genomic DNA. Translation: BAA15983.1.
PIRiF64986.
RefSeqiNP_416680.1. NC_000913.3.
WP_000241011.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75236; AAC75236; b2175.
BAA15983; BAA15983; BAA15983.
GeneIDi946686.
KEGGiecj:JW2163.
eco:b2175.
PATRICi32119705. VBIEscCol129921_2263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86610 Genomic DNA. Translation: BAA13140.1.
U00096 Genomic DNA. Translation: AAC75236.1.
AP009048 Genomic DNA. Translation: BAA15983.1.
PIRiF64986.
RefSeqiNP_416680.1. NC_000913.3.
WP_000241011.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1GNMR-A63-188[»]
ProteinModelPortaliP0AFV4.
SMRiP0AFV4. Positions 63-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261093. 195 interactions.
IntActiP0AFV4. 8 interactions.
STRINGi511145.b2175.

Protein family/group databases

MEROPSiC40.004.

Proteomic databases

PaxDbiP0AFV4.
PRIDEiP0AFV4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75236; AAC75236; b2175.
BAA15983; BAA15983; BAA15983.
GeneIDi946686.
KEGGiecj:JW2163.
eco:b2175.
PATRICi32119705. VBIEscCol129921_2263.

Organism-specific databases

EchoBASEiEB3829.
EcoGeneiEG14076. mepS.

Phylogenomic databases

eggNOGiENOG4107TT5. Bacteria.
COG0791. LUCA.
HOGENOMiHOG000229978.
InParanoidiP0AFV4.
KOiK13694.
OMAiWASRYMG.
PhylomeDBiP0AFV4.

Enzyme and pathway databases

UniPathwayiUPA00963.
BioCyciEcoCyc:G7147-MONOMER.
ECOL316407:JW2163-MONOMER.
MetaCyc:G7147-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AFV4.
PROiP0AFV4.

Family and domain databases

Gene3Di3.90.1720.10. 1 hit.
InterProiIPR000064. NLP_P60_dom.
[Graphical view]
PfamiPF00877. NLPC_P60. 1 hit.
[Graphical view]
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMEPS_ECOLI
AccessioniPrimary (citable) accession number: P0AFV4
Secondary accession number(s): O08016, P77685
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.