HMM Summary Page: TIGR01205

AccessionTIGR01205
NameD_ala_D_alaTIGR
FunctionD-alanine--D-alanine ligase
Trusted Cutoff245.65
Domain Trusted Cutoff245.65
Noise Cutoff95.55
Domain Noise Cutoff95.55
Isology Typesubfamily
EC Number6.3.2.4
HMM Length318
Mainrole CategoryCell envelope
Subrole CategoryBiosynthesis and degradation of murein sacculus and peptidoglycan
Gene Ontology TermGO:0008716: D-alanine-D-alanine ligase activity molecular_function
GO:0008716: D-alanine-D-alanine ligase activity molecular_function
GO:0008716: D-alanine-D-alanine ligase activity molecular_function
GO:0009252: peptidoglycan biosynthetic process biological_process
GO:0009252: peptidoglycan biosynthetic process biological_process
GO:0009252: peptidoglycan biosynthetic process biological_process
AuthorHaft DH
Entry DateMar 20 2001 10:30AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model.
ReferencesChanges in small numbers of amino acids, as demonstrated crystallographically, can alter specificity. DR HAMAP; MF_00047; 436 of 456
Genome PropertyGenProp0158: peptidoglycan(murein) biosynthesis (HMM)
GenProp0158: peptidoglycan(murein) biosynthesis (HMM)
GenProp0158: peptidoglycan(murein) biosynthesis (HMM)
GenProp0158: peptidoglycan(murein) biosynthesis (HMM)
GenProp0158: peptidoglycan(murein) biosynthesis (HMM)
GenProp0158: peptidoglycan(murein) biosynthesis (HMM)