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ECOLX:A0A023Z1P7
Contents
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 |
ECO:0000250 |
|
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 | ||||
enables |
GO:0004553 |
hydrolase activity, hydrolyzing O-glycosyl compounds |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009254 |
peptidoglycan turnover |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0019867 |
outer membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016829 |
lyase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0071555 |
cell wall organization |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009254 |
peptidoglycan turnover |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000129104 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016829 |
lyase activity |
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.
- ↑ 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
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