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9CAUD:A0A0K2CZX2
Contents
Species (Taxon ID) | Bacillus phage TsarBomba. (1690456) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | Murein transglycosylase A (ECO:0000313 with EMBL:ALA13018.1) | |
External Links | ||
UniProt | A0A0K2CZX2 | |
EMBL | KT224359 | |
RefSeq | YP_009206903.1 | |
GeneID | 26633229 | |
GO | GO:0019867 GO:0004553 GO:0009254 | |
InterPro | IPR010611 IPR009009 | |
Pfam | PF06725 | |
SUPFAM | SSF50685 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:2000966 |
peptidoglycan turnover |
ECO:0000250 |
UniProtKB:A0A023Z1P7 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. Since these sites 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, we can conclude that this protein in Bacillus phage TsarBomba is also a MltA protein with the same protein function. |
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 | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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