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P0AFS9

- MEPM_ECOLI

UniProt

P0AFS9 - MEPM_ECOLI

Protein

Murein DD-endopeptidase MepM

Gene

mepM

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    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

    Zinc, although calcium also allows some activity.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi314 – 3141ZincSequence Analysis

    GO - Molecular functioni

    1. endopeptidase activity Source: CACAO
    2. metal ion binding Source: UniProtKB-KW
    3. metalloendopeptidase activity Source: EcoCyc

    GO - Biological processi

    1. autolysis Source: EcoliWiki
    2. capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
    3. cytokinetic cell separation Source: EcoliWiki
    4. peptidoglycan metabolic process Source: EcoCyc

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10013. mepM.

    Subcellular locationi

    Cell inner membrane Curated; Single-pass membrane protein Curated
    Note: Uniform peripheral location, with partial enrichment at cell poles.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    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

    Expressioni

    Gene expression databases

    GenevestigatoriP0AFS9.

    Interactioni

    Protein-protein interaction databases

    STRINGi511145.b1856.

    Structurei

    3D structure databases

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

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 4020HelicalSequence AnalysisAdd
    BLAST

    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.
    KOiK01417.
    OMAiSSVLNQY.
    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

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    MQQIARSVAL AFNNLPRPHR VMLGSLTVLT LAVAVWRPYV YHRDATPIVK    50
    TIELEQNEIR SLLPEASEPI DQAAQEDEAI PQDELDDKIA GEAGVHEYVV 100
    STGDTLSSIL NQYGIDMGDI TQLAAADKEL RNLKIGQQLS WTLTADGELQ 150
    RLTWEVSRRE TRTYDRTAAN GFKMTSEMQQ GEWVNNLLKG TVGGSFVASA 200
    RNAGLTSAEV SAVIKAMQWQ MDFRKLKKGD EFAVLMSREM LDGKREQSQL 250
    LGVRLRSEGK DYYAIRAEDG KFYDRNGTGL AKGFLRFPTA KQFRISSNFN 300
    PRRTNPVTGR VAPHRGVDFA MPQGTPVLSV GDGEVVVAKR SGAAGYYVAI 350
    RHGRSYTTRY MHLRKILVKP GQKVKRGDRI ALSGNTGRST GPHLHYEVWI 400
    NQQAVNPLTA KLPRTEGLTG SDRREFLAQA KEIVPQLRFD 440
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901A → P in AAA81029. 1 PublicationCurated
    Sequence conflicti93 – 931A → T in AAA81029. 1 PublicationCurated
    Sequence conflicti121 – 1211T → S in AAA81029. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490118.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74926; AAC74926; b1856.
    BAA15664; BAA15664; BAA15664.
    GeneIDi12931358.
    946376.
    KEGGiecj:Y75_p1832.
    eco:b1856.
    PATRICi32119035. VBIEscCol129921_1935.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_416370.2. NC_000913.3.
    YP_490118.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0AFS9.
    SMRi P0AFS9. Positions 98-413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 511145.b1856.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74926 ; AAC74926 ; b1856 .
    BAA15664 ; BAA15664 ; BAA15664 .
    GeneIDi 12931358.
    946376.
    KEGGi ecj:Y75_p1832.
    eco:b1856.
    PATRICi 32119035. VBIEscCol129921_1935.

    Organism-specific databases

    EchoBASEi EB0013.
    EcoGenei EG10013. mepM.

    Phylogenomic databases

    eggNOGi COG0739.
    HOGENOMi HOG000281149.
    KOi K01417.
    OMAi SSVLNQY.
    OrthoDBi EOG61KBD1.
    PhylomeDBi P0AFS9.

    Enzyme and pathway databases

    UniPathwayi UPA00963 .
    BioCyci EcoCyc:EG10013-MONOMER.
    ECOL316407:JW5304-MONOMER.
    MetaCyc:EG10013-MONOMER.

    Miscellaneous databases

    PROi P0AFS9.

    Gene expression databases

    Genevestigatori P0AFS9.

    Family and domain databases

    Gene3Di 3.10.350.10. 1 hit.
    InterProi IPR011055. Dup_hybrid_motif.
    IPR018392. LysM_dom.
    IPR013731. OapA_N.
    IPR016047. Peptidase_M23.
    [Graphical view ]
    Pfami PF01476. LysM. 1 hit.
    PF08525. OapA_N. 1 hit.
    PF01551. Peptidase_M23. 1 hit.
    [Graphical view ]
    SMARTi SM00257. LysM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51261. SSF51261. 1 hit.
    SSF54106. SSF54106. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 77 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