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Protein

Murein DD-endopeptidase MepM

Gene

mepM

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. Partially suppresses an mepS disruption mutant.1 Publication

Cofactori

Zn2+1 Publication, Ca2+1 PublicationNote: Zinc, although calcium also allows some activity.1 Publication

Pathway: 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
Metal bindingi314 – 3141ZincSequence Analysis

GO - Molecular functioni

  • endopeptidase activity Source: CACAO
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: EcoCyc

GO - Biological processi

  • autolysis Source: EcoliWiki
  • capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
  • cell separation after cytokinesis Source: EcoliWiki
  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell wall biogenesis/degradation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10013-MONOMER.
ECOL316407:JW5304-MONOMER.
MetaCyc:EG10013-MONOMER.
UniPathwayiUPA00963.

Names & Taxonomyi

Protein namesi
Recommended name:
Murein DD-endopeptidase MepM (EC:3.4.24.-)
Alternative name(s):
Murein hydrolase MepM
ORFU
Gene namesi
Name:mepM
Synonyms:yebA
Ordered Locus Names:b1856, JW5304
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10013. mepM.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei21 – 4020HelicalSequence AnalysisAdd
BLAST
Topological domaini41 – 440400PeriplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells are shorter in a single mutant, while triple envC-nlpD-mepM disruptions have defects in septation and cell separation and form long filaments (15-fold longer) and further yet by the quadruple disruption mutant (envC-nlpD-mepM-ygeR, over 21-fold longer). Quadruple mutants are less sensitive to ampicillin lysis (PubMed:19525345). 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) (PubMed:23062283).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Murein DD-endopeptidase MepMPRO_0000026826Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi511145.b1856.

Structurei

3D structure databases

ProteinModelPortaliP0AFS9.
SMRiP0AFS9. Positions 98-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati98 – 14245LysMAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M23B family.Curated
Contains 1 LysM repeat.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0739.
HOGENOMiHOG000281149.
InParanoidiP0AFS9.
KOiK01417.
OMAiLPRMEGL.
OrthoDBiEOG61KBD1.
PhylomeDBiP0AFS9.

Family and domain databases

Gene3Di3.10.350.10. 1 hit.
InterProiIPR011055. Dup_hybrid_motif.
IPR018392. LysM_dom.
IPR013731. OapA_N.
IPR016047. Peptidase_M23.
[Graphical view]
PfamiPF01476. LysM. 1 hit.
PF08525. OapA_N. 1 hit.
PF01551. Peptidase_M23. 1 hit.
[Graphical view]
SMARTiSM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
SSF54106. SSF54106. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AFS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQIARSVAL AFNNLPRPHR VMLGSLTVLT LAVAVWRPYV YHRDATPIVK
60 70 80 90 100
TIELEQNEIR SLLPEASEPI DQAAQEDEAI PQDELDDKIA GEAGVHEYVV
110 120 130 140 150
STGDTLSSIL NQYGIDMGDI TQLAAADKEL RNLKIGQQLS WTLTADGELQ
160 170 180 190 200
RLTWEVSRRE TRTYDRTAAN GFKMTSEMQQ GEWVNNLLKG TVGGSFVASA
210 220 230 240 250
RNAGLTSAEV SAVIKAMQWQ MDFRKLKKGD EFAVLMSREM LDGKREQSQL
260 270 280 290 300
LGVRLRSEGK DYYAIRAEDG KFYDRNGTGL AKGFLRFPTA KQFRISSNFN
310 320 330 340 350
PRRTNPVTGR VAPHRGVDFA MPQGTPVLSV GDGEVVVAKR SGAAGYYVAI
360 370 380 390 400
RHGRSYTTRY MHLRKILVKP GQKVKRGDRI ALSGNTGRST GPHLHYEVWI
410 420 430 440
NQQAVNPLTA KLPRTEGLTG SDRREFLAQA KEIVPQLRFD
Length:440
Mass (Da):49,058
Last modified:December 20, 2005 - v1
Checksum:i30431410A5B1A7F7
GO

Sequence cautioni

The sequence AAA81029.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901A → P in AAA81029 (Ref. 4) Curated
Sequence conflicti93 – 931A → T in AAA81029 (Ref. 4) Curated
Sequence conflicti121 – 1211T → S in AAA81029 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74926.2.
AP009048 Genomic DNA. Translation: BAA15664.2.
U38702 Genomic DNA. Translation: AAA81029.1. Different initiation.
M77039 Genomic DNA. Translation: AAA24180.1.
RefSeqiNP_416370.2. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74926; AAC74926; b1856.
BAA15664; BAA15664; BAA15664.
GeneIDi946376.
KEGGiecj:Y75_p1832.
eco:b1856.
PATRICi32119035. VBIEscCol129921_1935.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74926.2.
AP009048 Genomic DNA. Translation: BAA15664.2.
U38702 Genomic DNA. Translation: AAA81029.1. Different initiation.
M77039 Genomic DNA. Translation: AAA24180.1.
RefSeqiNP_416370.2. NC_000913.3.

3D structure databases

ProteinModelPortaliP0AFS9.
SMRiP0AFS9. Positions 98-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi511145.b1856.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74926; AAC74926; b1856.
BAA15664; BAA15664; BAA15664.
GeneIDi946376.
KEGGiecj:Y75_p1832.
eco:b1856.
PATRICi32119035. VBIEscCol129921_1935.

Organism-specific databases

EchoBASEiEB0013.
EcoGeneiEG10013. mepM.

Phylogenomic databases

eggNOGiCOG0739.
HOGENOMiHOG000281149.
InParanoidiP0AFS9.
KOiK01417.
OMAiLPRMEGL.
OrthoDBiEOG61KBD1.
PhylomeDBiP0AFS9.

Enzyme and pathway databases

UniPathwayiUPA00963.
BioCyciEcoCyc:EG10013-MONOMER.
ECOL316407:JW5304-MONOMER.
MetaCyc:EG10013-MONOMER.

Miscellaneous databases

PROiP0AFS9.

Family and domain databases

Gene3Di3.10.350.10. 1 hit.
InterProiIPR011055. Dup_hybrid_motif.
IPR018392. LysM_dom.
IPR013731. OapA_N.
IPR016047. Peptidase_M23.
[Graphical view]
PfamiPF01476. LysM. 1 hit.
PF08525. OapA_N. 1 hit.
PF01551. Peptidase_M23. 1 hit.
[Graphical view]
SMARTiSM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
SSF54106. SSF54106. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Robison K., O'Keeffe T., Church G.M.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-182.
    Strain: K12 / EMG2.
  5. "Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB."
    Karow M.L., Georgopoulos C.
    J. Bacteriol. 174:702-710(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-440.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli."
    Uehara T., Dinh T., Bernhardt T.G.
    J. Bacteriol. 191:5094-5107(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / TB28.
  7. "Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12."
    Singh S.K., SaiSree L., Amrutha R.N., Reddy M.
    Mol. Microbiol. 86:1036-1051(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A MUREIN DD-ENDOPEPTIDASE, COFACTOR, DISRUPTION PHENOTYPE.
    Strain: K12.

Entry informationi

Entry nameiMEPM_ECOLI
AccessioniPrimary (citable) accession number: P0AFS9
Secondary accession number(s): O07981, P24204, P76283
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: June 24, 2015
This is version 83 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

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. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.