GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

NEIME:A0A0G4BQJ3

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Neisseria meningitidis. (487)
Gene Name(s) mltA (ECO:0000313 with EMBL:AKM89960.1)
Protein Name(s) Membrane-bound lytic murein transglycosylase A (ECO:0000313 with EMBL:AKM89960.1)
External Links
UniProt A0A0G4BQJ3
EMBL CP007667
EnsemblBacteria AKM89960
Proteomes UP000035643
GO GO:0019867
GO:0004553
GO:0016829
GO:0009254
Gene3D 2.40.40.10
InterPro IPR010611
IPR005300
IPR009009
Pfam PF06725
PF03562
SMART SM00925
SUPFAM SSF50685

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005300
InterPro:IPR010611

F

Seeded From UniProt

GO:0009254

peptidoglycan turnover

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010611

P

Seeded From UniProt

GO:0019867

outer membrane

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010611

C

Seeded From UniProt

GO:2000966

regulation of cell wall polysaccharide catabolic process

PMID:16618494[1]

ISS: Inferred from Sequence Similarity

UniProtKB:A0A023Z1P7


P

MltA is a lytic transglycosylase of Gram-negative bacteria that cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan. We have determined the crystal structures of MltA from Neisseria gonorrhoeae and Escherichia coli (NgMltA and EcMltA), which have only 21.5% sequence identity but have 2 main domains separated by a deep grove pointing that they are both MltA proteins.

complete
CACAO 11435

Notes

References

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

  1. Powell, AJ et al. (2006) Crystal structures of the lytic transglycosylase MltA from N.gonorrhoeae and E.coli: insights into interdomain movements and substrate binding. J. Mol. Biol. 359 122-36 PubMed GONUTS page