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BACSU:DACA

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Species (Taxon ID) Bacillus subtilis (strain 168). (224308)
Gene Name(s) dacA
Protein Name(s) D-alanyl-D-alanine carboxypeptidase DacA

CPase DD-carboxypeptidase DD-peptidase Penicillin-binding protein 5 PBP-5

External Links
UniProt P08750
EMBL D26185
AL009126
M13766
PIR S66040
RefSeq NP_387891.1
ProteinModelPortal P08750
SMR P08750
STRING 224308.BSU00100
ChEMBL CHEMBL3112381
MEROPS S11.001
PaxDb P08750
EnsemblBacteria CAB11786
GeneID 940000
KEGG bsu:BSU00100
PATRIC 18971479
GenoList BSU00100
eggNOG COG1686
HOGENOM HOG000086625
InParanoid P08750
KO K07258
OMA LACSIFM
OrthoDB EOG657JCD
PhylomeDB P08750
BioCyc BSUB:BSU00100-MONOMER
UniPathway UPA00219
Proteomes UP000001570
GO GO:0005618
GO:0005576
GO:0009002
GO:0071555
GO:0009252
GO:0008360
Gene3D 2.60.410.10
3.40.710.10
InterPro IPR012338
IPR015956
IPR018044
IPR012907
IPR001967
Pfam PF07943
PF00768
PRINTS PR00725
SMART SM00936
SUPFAM SSF56601
SSF69189

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

PMID:3087956[1]

ECO:0000247

sequence alignment evidence used in manual assertion

UniProtKB:P0AEB2

F

Seeded From UniProt

complete

enables

GO:0004175

endopeptidase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12015
PANTHER:PTN000491515

F

Seeded From UniProt

complete

enables

GO:0004180

carboxypeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015956

F

Seeded From UniProt

complete

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

PMID:3087956[1]

ECO:0000247

UniProtKB:P0AEB2


F

There are several regions of similarity between the amino acid sequences of B. subtilis PBP 5 and E. coli PBP 5 (4) (Fig. 2), accounting for an overall 25% identity. This suggests (8) that these proteins are homologous. The similar regions (Fig. 2) include one around the active-site serine residues (positions 36 and 44 for B. subtilis and E. coli, respectively), extending from positions 7 to 56 in B. subtilis PBP 5 (47% identical amino acids).

complete
CACAO 2809

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001967
InterPro:IPR012907
InterPro:IPR015956
InterPro:IPR018044
InterPro:IPR037167

P

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001967
InterPro:IPR012907
InterPro:IPR018044
InterPro:IPR037167

F

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.4.16.4

F

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0133

P

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0134
UniProtKB-SubCell:SL-0041

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964

C

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0961

P

Seeded From UniProt

complete

enables

GO:0004180

carboxypeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0121

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0573
UniPathway:UPA00219

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Todd, JA et al. (1986) Reduced heat resistance of mutant spores after cloning and mutagenesis of the Bacillus subtilis gene encoding penicillin-binding protein 5. J. Bacteriol. 167 257-64 PubMed GONUTS page
  2. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page