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ECOLI:MEPM

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) mepM (synonyms: yebA)
Protein Name(s) Murein DD-endopeptidase MepM

Murein hydrolase MepM ORFU

External Links
UniProt P0AFS9
EMBL U00096
AP009048
U38702
M77039
RefSeq NP_416370.2
WP_001184045.1
ProteinModelPortal P0AFS9
SMR P0AFS9
BioGrid 4260352
STRING 511145.b1856
MEROPS M23.011
PaxDb P0AFS9
EnsemblBacteria AAC74926
BAA15664
GeneID 946376
KEGG ecj:JW5304
eco:b1856
PATRIC 32119035
EchoBASE EB0013
EcoGene EG10013
eggNOG ENOG4105DR5
COG0739
HOGENOM HOG000281149
InParanoid P0AFS9
KO K19304
OMA EYQTVYM
OrthoDB EOG61KBD1
PhylomeDB P0AFS9
BioCyc EcoCyc:EG10013-MONOMER
ECOL316407:JW5304-MONOMER
MetaCyc:EG10013-MONOMER
UniPathway UPA00963
PRO PR:P0AFS9
Proteomes UP000000318
UP000000625
GO GO:0016021
GO:0005886
GO:0004175
GO:0046872
GO:0004222
GO:0001896
GO:0045227
GO:0000920
GO:0071555
GO:0000270
Gene3D 3.10.350.10
InterPro IPR011055
IPR018392
IPR013731
IPR016047
Pfam PF01476
PF08525
PF01551
SMART SM00257
SUPFAM SSF51261
SSF54106
PROSITE PS51782

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009254

peptidoglycan turnover

PMID:23062283[1]

ECO:0000315

P

Fig 4, Fig 3, Fig 5 C & D, Fig 6

complete
CACAO 5432

GO:0004175

endopeptidase activity

PMID:23062283[1]

ECO:0000314

F

Fig 4

complete
CACAO 5433

GO:0004175

endopeptidase activity

PMID:23062283[1]

ECO:0000314

F

Fig 4

complete
CACAO 5430

enables

GO:0004175

endopeptidase activity

PMID:23062283[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10013
PANTHER:PTN002729049
UniProtKB:O33599

F

Seeded From UniProt

complete

involved_in

GO:0001896

autolysis

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10013
EcoGene:EG12111
EcoGene:EG12297
EcoGene:EG13048
PANTHER:PTN002729094

P

Seeded From UniProt

complete

involved_in

GO:0000920

septum digestion after cytokinesis

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10013
EcoGene:EG12111
EcoGene:EG12297
EcoGene:EG13048
PANTHER:PTN002729094

P

Seeded From UniProt

complete

involved_in

GO:0001896

autolysis

PMID:19525345[3]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P0ADA3
UniProtKB:P37690
UniProtKB:Q46798

P

Seeded From UniProt

complete

involved_in

GO:0000920

septum digestion after cytokinesis

PMID:19525345[3]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P37690

P

Seeded From UniProt

complete

involved_in

GO:0000920

septum digestion after cytokinesis

PMID:19525345[3]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P0ADA3
UniProtKB:P37690
UniProtKB:Q46798

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:19525345[3]

ECO:0000245

automatically integrated combinatorial evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

PMID:23062283[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000270

peptidoglycan metabolic process

PMID:23062283[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0961

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0045227

capsule polysaccharide biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00963

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 Singh, SK et al. (2012) Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12. Mol. Microbiol. 86 1036-51 PubMed GONUTS page
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Uehara, T et al. (2009) LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli. J. Bacteriol. 191 5094-107 PubMed GONUTS page