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

ECOLX:A0A023Z1P7

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli O145:H28 str. RM12581. (1248823)
Gene Name(s) mltA (ECO:0000313 with EMBL:AHY72152.1)
Protein Name(s) Membrane-bound lytic murein transglycosylase A (ECO:0000313 with EMBL:AHY72152.1)
External Links
UniProt A0A023Z1P7
EMBL CP007136
RefSeq WP_000678646.1
ProteinModelPortal A0A023Z1P7
EnsemblBacteria AHY72152
OMA KREDMSM
Proteomes UP000025231
GO GO:0019867
GO:0004553
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 ECO ID ECO term name with/from Aspect Extension Notes Status
GO:2000966

regulation of cell wall polysaccharide catabolic process

PMID:16615077[1]

ECO:0000250

UniProtKB:A0A0G4BQJ3


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 11434

enables

GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005300
InterPro:IPR010611

F

Seeded From UniProt

complete

involved_in

GO:0009254

peptidoglycan turnover

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010611

P

Seeded From UniProt

complete

part_of

GO:0019867

outer membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010611

C

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0961

P

Seeded From UniProt

complete

involved_in

GO:0009254

peptidoglycan turnover

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000129104

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000129104

F

Seeded From UniProt

complete

Notes

References

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

  1. Sotelo-Mundo, RR et al. (2006) Crystal structures of thymidylate synthase mutant R166Q: structural basis for the nearly complete loss of catalytic activity. J. Biochem. Mol. Toxicol. 20 88-92 PubMed GONUTS page