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ECOLI:SLT

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) slt (synonyms: sltY)
Protein Name(s) Soluble lytic murein transglycosylase

Exomuramidase Peptidoglycan lytic exotransglycosylase Slt70

External Links
UniProt P0AGC3
EMBL M69185
U14003
U00096
AP009048
J01715
PIR S56616
RefSeq NP_418809.4
YP_492522.1
PDB 1QSA
1QTE
1SLY
PDBsum 1QSA
1QTE
1SLY
ProteinModelPortal P0AGC3
SMR P0AGC3
IntAct P0AGC3
STRING 511145.b4392
CAZy GH23
PaxDb P0AGC3
PRIDE P0AGC3
EnsemblBacteria AAC77345
BAE78381
GeneID 12931805
948908
KEGG ecj:Y75_p4276
eco:b4392
PATRIC 32124402
EchoBASE EB0943
EcoGene EG10950
eggNOG COG0741
HOGENOM HOG000275388
InParanoid P0AGC3
KO K08309
OMA VDWHERY
OrthoDB EOG6S52QZ
PhylomeDB P0AGC3
BioCyc EcoCyc:EG10950-MONOMER
ECOL316407:JW4355-MONOMER
MetaCyc:EG10950-MONOMER
EvolutionaryTrace P0AGC3
PRO PR:P0AGC3
Proteomes UP000000318
UP000000625
Genevestigator P0AGC3
GO GO:0016020
GO:0030288
GO:0016837
GO:0004553
GO:0008933
GO:0071555
GO:0000270
Gene3D 1.10.1240.20
1.25.20.10
InterPro IPR023346
IPR016026
IPR012289
IPR008939
IPR008258
IPR000189
Pfam PF01464
PF14718
SUPFAM SSF48435
SSF53955
PROSITE PS00922

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0071555

cell wall organization

PMID:9287002[1]

ECO:0000316

UniProtKB:P0A908 UniProtKB:P41052


P

Table 2

complete
CACAO 3787

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:1938883[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008933

lytic transglycosylase activity

PMID:1938883[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:24140104[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:15911532[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009274

peptidoglycan-based cell wall

PMID:1885544[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

PMID:1938883[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

PMID:1400320[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

PMID:7018908[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

PMID:357[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

PMID:25480295[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008933

lytic transglycosylase activity

PMID:7018908[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008933

lytic transglycosylase activity

PMID:357[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008933

lytic transglycosylase activity

PMID:23421439[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008932

lytic endotransglycosylase activity

PMID:23421439[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000270

peptidoglycan metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000189

P

Seeded From UniProt

complete

enables

GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008939
InterPro:IPR012289
InterPro:IPR037061

F

Seeded From UniProt

complete

enables

GO:0008933

lytic transglycosylase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000189

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:IPR000189

C

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008939
InterPro:IPR012289
InterPro:IPR037061

C

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0574
UniProtKB-SubCell:SL-0200

C

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

Notes

References

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

  1. Lommatzsch, J et al. (1997) Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli. J. Bacteriol. 179 5465-70 PubMed GONUTS page
  2. 2.0 2.1 2.2 Engel, H et al. (1991) Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase. J. Bacteriol. 173 6773-82 PubMed GONUTS page
  3. Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page
  4. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  5. Walderich, B & Höltje, JV (1991) Subcellular distribution of the soluble lytic transglycosylase in Escherichia coli. J. Bacteriol. 173 5668-76 PubMed GONUTS page
  6. Templin, MF et al. (1992) A murein hydrolase is the specific target of bulgecin in Escherichia coli. J. Biol. Chem. 267 20039-43 PubMed GONUTS page
  7. 7.0 7.1 Beachey, EH et al. (1981) Exoenzymatic activity of transglycosylase isolated from Escherichia coli. Eur. J. Biochem. 116 355-8 PubMed GONUTS page
  8. 8.0 8.1 Höltje, JV et al. (1975) Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124 1067-76 PubMed GONUTS page
  9. Cho, H et al. (2014) Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery. Cell 159 1300-11 PubMed GONUTS page
  10. 10.0 10.1 Lee, M et al. (2013) Reactions of all Escherichia coli lytic transglycosylases with bacterial cell wall. J. Am. Chem. Soc. 135 3311-4 PubMed GONUTS page