Peptidoglycan-N-acetylmuramic acid deacetylase PdaA
Details
- Name
- Peptidoglycan-N-acetylmuramic acid deacetylase PdaA
- Kind
- protein
- Synonyms
- 3.5.1.-
- Peptidoglycan MurNAc deacetylase
- yfjS
- Gene Name
- pdaA
- UniProtKB Entry
- O34928Swiss-Prot
- Organism
- Bacillus subtilis (strain 168)
- NCBI Taxonomy ID
- 224308
- Amino acid sequence
>lcl|BSEQ0011434|Peptidoglycan-N-acetylmuramic acid deacetylase PdaA MKWMCSICCAAVLLAGGAAQAEAVPNEPINWGFKRSVNHQPPDAGKQLNSLIEKYDAFYL GNTKEKTIYLTFDNGYENGYTPKVLDVLKKHRVTGTFFVTGHFVKDQPQLIKRMSDEGHI IGNHSFHHPDLTTKTADQIQDELDSVNEEVYKITGKQDNLYLRPPRGVFSEYVLKETKRL GYQTVFWSVAFVDWKINNQKGKKYAYDHMIKQAHPGAIYLLHTVSRDNAEALDDAITDLK KQGYTFKSIDDLMFEKEMRLPSL
- Number of residues
- 263
- Molecular Weight
- 30069.06
- Theoretical pI
- 7.7
- GO Classification
- Functionshydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / metal ion bindingProcessescarbohydrate metabolic process / cell wall organization / sporulation resulting in formation of a cellular spore
- General Function
- Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N-acetylchitohexaose) as a substrate.
- Specific Function
- deacetylase activity
- Pfam Domain Function
- Polysacc_deac_1 (PF01522)
- Signal Regions
- 1-23
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0011435|Peptidoglycan-N-acetylmuramic acid deacetylase PdaA (pdaA) ATGAAGTGGATGTGTTCAATATGCTGCGCCGCCGTATTGCTTGCCGGAGGTGCAGCACAG GCGGAAGCGGTGCCGAATGAGCCGATTAATTGGGGCTTTAAACGAAGTGTCAATCATCAG CCGCCAGATGCCGGGAAGCAGCTGAACAGTTTAATTGAAAAATATGACGCGTTTTATTTA GGGAATACAAAGGAAAAAACGATTTACTTAACGTTTGATAACGGATATGAAAATGGCTAT ACGCCAAAAGTGCTTGATGTCTTAAAAAAACATCGCGTAACAGGAACGTTTTTTGTCACC GGGCATTTCGTAAAGGACCAGCCTCAGCTGATCAAACGAATGTCAGATGAGGGCCATATT ATCGGCAATCATTCCTTTCACCATCCGGATTTAACGACAAAAACAGCTGATCAGATTCAG GATGAACTTGATTCAGTCAACGAAGAGGTTTATAAAATTACGGGAAAGCAGGACAACCTG TATTTGCGTCCGCCGCGCGGCGTGTTCAGTGAGTACGTACTGAAAGAAACGAAACGCCTC GGCTATCAAACCGTTTTCTGGTCGGTCGCTTTTGTTGATTGGAAAATCAACAACCAAAAG GGAAAGAAATATGCCTACGATCATATGATCAAGCAGGCGCACCCGGGAGCCATTTACCTG CTTCACACCGTATCGAGGGACAATGCAGAAGCGCTGGATGACGCGATTACAGATCTGAAA AAACAGGGCTACACTTTTAAAAGCATTGATGATCTGATGTTTGAGAAAGAAATGAGGCTG CCGTCTTTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O34928 UniProtKB Entry Name PDAA_BACSU GenBank Protein ID 2626811 GenBank Gene ID D83967 PDB ID(s) 1NY1, 1W17, 1W1A, 1W1B KEGG ID bsu:BSU07980 NCBI Gene ID 936136 - General References
- Yamamoto H, Uchiyama S, Sekiguchi J: Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees region of the Bacillus subtilis chromosome containing genes for trehalose metabolism and acetoin utilization. Microbiology. 1996 Nov;142 ( Pt 11):3057-65. [Article]
- Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Cordani JJ, Connerton IF, Cummings NJ, Daniel RA, Denziot F, Devine KM, Dusterhoft A, Ehrlich SD, Emmerson PT, Entian KD, Errington J, Fabret C, Ferrari E, Foulger D, Fritz C, Fujita M, Fujita Y, Fuma S, Galizzi A, Galleron N, Ghim SY, Glaser P, Goffeau A, Golightly EJ, Grandi G, Guiseppi G, Guy BJ, Haga K, Haiech J, Harwood CR, Henaut A, Hilbert H, Holsappel S, Hosono S, Hullo MF, Itaya M, Jones L, Joris B, Karamata D, Kasahara Y, Klaerr-Blanchard M, Klein C, Kobayashi Y, Koetter P, Koningstein G, Krogh S, Kumano M, Kurita K, Lapidus A, Lardinois S, Lauber J, Lazarevic V, Lee SM, Levine A, Liu H, Masuda S, Mauel C, Medigue C, Medina N, Mellado RP, Mizuno M, Moestl D, Nakai S, Noback M, Noone D, O'Reilly M, Ogawa K, Ogiwara A, Oudega B, Park SH, Parro V, Pohl TM, Portelle D, Porwollik S, Prescott AM, Presecan E, Pujic P, Purnelle B, Rapoport G, Rey M, Reynolds S, Rieger M, Rivolta C, Rocha E, Roche B, Rose M, Sadaie Y, Sato T, Scanlan E, Schleich S, Schroeter R, Scoffone F, Sekiguchi J, Sekowska A, Seror SJ, Serror P, Shin BS, Soldo B, Sorokin A, Tacconi E, Takagi T, Takahashi H, Takemaru K, Takeuchi M, Tamakoshi A, Tanaka T, Terpstra P, Togoni A, Tosato V, Uchiyama S, Vandebol M, Vannier F, Vassarotti A, Viari A, Wambutt R, Wedler H, Weitzenegger T, Winters P, Wipat A, Yamamoto H, Yamane K, Yasumoto K, Yata K, Yoshida K, Yoshikawa HF, Zumstein E, Yoshikawa H, Danchin A: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. [Article]
- Fukushima T, Yamamoto H, Atrih A, Foster SJ, Sekiguchi J: A polysaccharide deacetylase gene (pdaA) is required for germination and for production of muramic delta-lactam residues in the spore cortex of Bacillus subtilis. J Bacteriol. 2002 Nov;184(21):6007-15. [Article]
- Gilmore ME, Bandyopadhyay D, Dean AM, Linnstaedt SD, Popham DL: Production of muramic delta-lactam in Bacillus subtilis spore peptidoglycan. J Bacteriol. 2004 Jan;186(1):80-9. [Article]
- Fukushima T, Kitajima T, Sekiguchi J: A polysaccharide deacetylase homologue, PdaA, in Bacillus subtilis acts as an N-acetylmuramic acid deacetylase in vitro. J Bacteriol. 2005 Feb;187(4):1287-92. [Article]
- Blair DE, van Aalten DM: Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine. FEBS Lett. 2004 Jul 16;570(1-3):13-9. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N-acetyl-alpha-D-glucosamine experimental unknown target Details