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P0AFS9 (MEPM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Murein DD-endopeptidase MepM

EC=3.4.24.-
Alternative name(s):
Murein hydrolase MepM
ORFU
Gene names
Name:mepM
Synonyms:yebA
Ordered Locus Names:b1856, JW5304
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Cofactor

Zinc, although calcium also allows some activity. Ref.7

Pathway

Cell wall biogenesis; cell wall polysaccharide biosynthesis.

Subcellular location

Cell inner membrane; Single-pass membrane protein Potential. Note: Uniform peripheral location, with partial enrichment at cell poles. Ref.6

Disruption phenotype

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 (Ref.6). 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) (Ref.7). Ref.6 Ref.7

Sequence similarities

Belongs to the peptidase M23B family.

Contains 1 LysM repeat.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Murein DD-endopeptidase MepM
PRO_0000026826

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4020Helical; Potential
Topological domain41 – 440400Periplasmic Potential
Repeat98 – 14245LysM

Sites

Metal binding3141Zinc Potential

Experimental info

Sequence conflict901A → P in AAA81029. Ref.4
Sequence conflict931A → T in AAA81029. Ref.4
Sequence conflict1211T → S in AAA81029. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P0AFS9 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 30431410A5B1A7F7

FASTA44049,058
        10         20         30         40         50         60 
MQQIARSVAL AFNNLPRPHR VMLGSLTVLT LAVAVWRPYV YHRDATPIVK TIELEQNEIR 

        70         80         90        100        110        120 
SLLPEASEPI DQAAQEDEAI PQDELDDKIA GEAGVHEYVV STGDTLSSIL NQYGIDMGDI 

       130        140        150        160        170        180 
TQLAAADKEL RNLKIGQQLS WTLTADGELQ RLTWEVSRRE TRTYDRTAAN GFKMTSEMQQ 

       190        200        210        220        230        240 
GEWVNNLLKG TVGGSFVASA RNAGLTSAEV SAVIKAMQWQ MDFRKLKKGD EFAVLMSREM 

       250        260        270        280        290        300 
LDGKREQSQL LGVRLRSEGK DYYAIRAEDG KFYDRNGTGL AKGFLRFPTA KQFRISSNFN 

       310        320        330        340        350        360 
PRRTNPVTGR VAPHRGVDFA MPQGTPVLSV GDGEVVVAKR SGAAGYYVAI RHGRSYTTRY 

       370        380        390        400        410        420 
MHLRKILVKP GQKVKRGDRI ALSGNTGRST GPHLHYEVWI NQQAVNPLTA KLPRTEGLTG 

       430        440 
SDRREFLAQA KEIVPQLRFD 

« Hide

References

« Hide 'large scale' references
[1]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_416370.2. NC_000913.3.
YP_490118.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AFS9.
SMRP0AFS9. Positions 98-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b1856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74926; AAC74926; b1856.
BAA15664; BAA15664; BAA15664.
GeneID12931358.
946376.
KEGGecj:Y75_p1832.
eco:b1856.
PATRIC32119035. VBIEscCol129921_1935.

Organism-specific databases

EchoBASEEB0013.
EcoGeneEG10013. mepM.

Phylogenomic databases

eggNOGCOG0739.
HOGENOMHOG000281149.
KOK01417.
OMASSVLNQY.
OrthoDBEOG61KBD1.
PhylomeDBP0AFS9.

Enzyme and pathway databases

BioCycEcoCyc:EG10013-MONOMER.
ECOL316407:JW5304-MONOMER.
MetaCyc:EG10013-MONOMER.
UniPathwayUPA00963.

Gene expression databases

GenevestigatorP0AFS9.

Family and domain databases

Gene3D3.10.350.10. 1 hit.
InterProIPR011055. Dup_hybrid_motif.
IPR018392. LysM_dom.
IPR013731. OapA_N.
IPR016047. Peptidase_M23.
[Graphical view]
PfamPF01476. LysM. 1 hit.
PF08525. OapA_N. 1 hit.
PF01551. Peptidase_M23. 1 hit.
[Graphical view]
SMARTSM00257. LysM. 1 hit.
[Graphical view]
SUPFAMSSF51261. SSF51261. 1 hit.
SSF54106. SSF54106. 1 hit.
ProtoNetSearch...

Other

PROP0AFS9.

Entry information

Entry nameMEPM_ECOLI
AccessionPrimary (citable) accession number: P0AFS9
Secondary accession number(s): O07981, P24204, P76283
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene