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ECOLI:MRAY

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) mraY (synonyms: murX)
Protein Name(s) Phospho-N-acetylmuramoyl-pentapeptide-transferase

UDP-MurNAc-pentapeptide phosphotransferase

External Links
UniProt P0A6W3
EMBL X51584
X55034
U00096
AP009048
PIR S08395
RefSeq NP_414629.1
YP_488392.1
ProteinModelPortal P0A6W3
SMR P0A6W3
STRING 511145.b0087
BindingDB P0A6W3
ChEMBL CHEMBL3957
EnsemblBacteria AAC73198
BAB96655
GeneID 12932484
944814
KEGG ecj:Y75_p0086
eco:b0087
PATRIC 32115279
EchoBASE EB0599
EcoGene EG10604
eggNOG COG0472
HOGENOM HOG000275122
InParanoid P0A6W3
KO K01000
OMA HQNKKDT
OrthoDB EOG69GZPZ
PhylomeDB P0A6W3
BioCyc EcoCyc:PHOSNACMURPENTATRANS-MONOMER
ECOL316407:JW0085-MONOMER
MetaCyc:PHOSNACMURPENTATRANS-MONOMER
UniPathway UPA00219
PRO PR:P0A6W3
Proteomes UP000000318
UP000000625
Genevestigator P0A6W3
GO GO:0016021
GO:0005886
GO:0008963
GO:0051992
GO:0007049
GO:0051301
GO:0071555
GO:0009252
GO:0008360
HAMAP MF_00038
InterPro IPR000715
IPR003524
IPR018480
PANTHER PTHR22926
Pfam PF00953
PF10555
TIGRFAMs TIGR00445
PROSITE PS01347
PS01348

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016021

integral to membrane

PMID:19892831[1]

ECO:0000255

PMID:7108955[2]


C

Figure 2 shows the hydropathy plot of E. coli MraY. The hydropathy plot model was originally developed by Kyte & Doolittle (1982) (PMID:7108955[2])

complete

involved_in

GO:0071555

cell wall organization

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10840
PANTHER:PTN000531998
UniProtKB:Q9X1N5

P

Seeded From UniProt

complete

involved_in

GO:0044038

cell wall macromolecule biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10840
PANTHER:PTN000531998
UniProtKB:Q9X1N5

P

Seeded From UniProt

complete

enables

GO:0016780

phosphotransferase activity, for other substituted phosphate groups

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10840
PANTHER:PTN000531998
UniProtKB:P9WMW5
UniProtKB:Q9X1N5

F

Seeded From UniProt

complete

enables

GO:0008963

phospho-N-acetylmuramoyl-pentapeptide-transferase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10604
PANTHER:PTN000532041

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10840
PANTHER:PTN000531998

C

Seeded From UniProt

complete

enables

GO:0008963

phospho-N-acetylmuramoyl-pentapeptide-transferase activity

PMID:1846850[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:215212[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008963

phospho-N-acetylmuramoyl-pentapeptide-transferase activity

PMID:215212[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008963

phospho-N-acetylmuramoyl-pentapeptide-transferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000715
InterPro:IPR003524

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003524

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000715

C

Seeded From UniProt

complete

enables

GO:0051992

UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.8.13

F

Seeded From UniProt

complete

enables

GO:0008963

phospho-N-acetylmuramoyl-pentapeptide-transferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.8.13

F

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000050410

P

Seeded From UniProt

complete

enables

GO:0008963

phospho-N-acetylmuramoyl-pentapeptide-transferase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000050410

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000050410

C

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

C

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0573
UniPathway:UPA00219

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0133

P

Seeded From UniProt

complete

involved_in

GO:0007049

cell cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0131

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

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

involved_in

GO:0051301

cell division

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0132

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

Notes

References

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

  1. Homi, S et al. (2009) The peptidoglycan biosynthesis genes MurA and MraY are related to chloroplast division in the moss Physcomitrella patens. Plant Cell Physiol. 50 2047-56 PubMed GONUTS page
  2. 2.0 2.1 Kyte, J & Doolittle, RF (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 105-32 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Ikeda, M et al. (1991) The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase. J. Bacteriol. 173 1021-6 PubMed GONUTS page
  5. 5.0 5.1 Geis, A & Plapp, R (1978) Phospho-N-acetylmuramoyl-pentapeptide-transferase of Escherichia coli K12. Properties of the membrane-bound and the extracted and partially purified enzyme. Biochim. Biophys. Acta 527 414-24 PubMed GONUTS page