ECOLI:DACA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dacA (synonyms: pfv)
Protein Name(s)	D-alanyl-D-alanine carboxypeptidase DacA DD-carboxypeptidase DD-peptidase Beta-lactamase Penicillin-binding protein 5 PBP-5
External Links
UniProt	P0AEB2
EMBL	X06479 M18276 U82598 U00096 AP009048 L07636
PIR	A28536
RefSeq	NP_415165.1 YP_488923.1
PDB	1HD8 1NJ4 1NZO 1NZU 1SDN 1Z6F 3BEB 3BEC 3MZD 3MZE 3MZF
PDBsum	1HD8 1NJ4 1NZO 1NZU 1SDN 1Z6F 3BEB 3BEC 3MZD 3MZE 3MZF
ProteinModelPortal	P0AEB2
SMR	P0AEB2
DIP	DIP-47947N
IntAct	P0AEB2
MINT	MINT-1247273
STRING	511145.b0632
ChEMBL	CHEMBL2354204
DrugBank	DB00274 DB01329 DB01331
MEROPS	S11.008
PhosSite	P0809377
PaxDb	P0AEB2
PRIDE	P0AEB2
EnsemblBacteria	AAC73733 BAA35275
GeneID	12931704 945222
KEGG	ecj:Y75_p0622 eco:b0632
PATRIC	32116445
EchoBASE	EB0197
EcoGene	EG10201
eggNOG	COG1686
HOGENOM	HOG000086623
InParanoid	P0AEB2
KO	K07258
OMA	KIYSERE
OrthoDB	EOG6RJV2H
PhylomeDB	P0AEB2
BioCyc	EcoCyc:EG10201-MONOMER ECOL316407:JW0627-MONOMER MetaCyc:EG10201-MONOMER
UniPathway	UPA00219
EvolutionaryTrace	P0AEB2
PRO	PR:P0AEB2
Proteomes	UP000000318 UP000000625
Genevestigator	P0AEB2
GO	GO:0005887 GO:0008800 GO:0004180 GO:0008658 GO:0009002 GO:0051301 GO:0044036 GO:0071555 GO:0009252 GO:0000270 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	Notes	Status
enables	GO:0009002	serine-type D-Ala-D-Ala carboxypeptidase activity	PMID:17685588^[1]	ECO:0000314	direct assay evidence used in manual assertion		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:0009002	serine-type D-Ala-D-Ala carboxypeptidase activity	PMID:368033^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
	GO:0008658	penicillin binding	PMID:10692378^[4]	ECO:0000315			F	Fig 4 and Table 2 Lack of PBP 5 produces irregular shape and size in cells	complete CACAO 3677
enables	GO:0009002	serine-type D-Ala-D-Ala carboxypeptidase activity	PMID:1740130^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
	GO:0009002	serine-type D-Ala-D-Ala carboxypeptidase activity	PMID:17685588^[1]	ECO:0000314			F	DD carboxypeptidase activity was demonstrated with a fluorescent assay. Figure 3 demonstrates pH profiling and optimal PBP5 catalysis.	complete CACAO 8328
part_of	GO:0005887	integral component of plasma membrane	PMID:319999^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0044036	cell wall macromolecule metabolic process	PMID:351612^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0044036	cell wall macromolecule metabolic process	PMID:7002918^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0009002	serine-type D-Ala-D-Ala carboxypeptidase activity	PMID:14750804^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008658	penicillin binding	PMID:7002918^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	PMID:9324260^[10]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P00811 UniProtKB:P02918 UniProtKB:P0AD70	P	Seeded From UniProt	complete
enables	GO:0004180	carboxypeptidase activity	PMID:351612^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004180	carboxypeptidase activity	PMID:7002918^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000270	peptidoglycan metabolic process	PMID:351612^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000270	peptidoglycan metabolic process	PMID:7002918^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	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
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
enables	GO:0008800	beta-lactamase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.5.2.6	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:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0997 UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0037	C	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
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
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
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	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
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
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Notes

References

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

↑ ^1.0 ^1.1 Zhang, W et al. (2007) Catalytic mechanism of penicillin-binding protein 5 of Escherichia coli. Biochemistry 46 10113-21 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Matsuhashi, M et al. (1979) Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity. J. Bacteriol. 137 644-7 PubMed GONUTS page
↑ Nelson, DE & Young, KD (2000) Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli. J. Bacteriol. 182 1714-21 PubMed GONUTS page
↑ van der Linden, MP et al. (1992) Cytoplasmic high-level expression of a soluble, enzymatically active form of the Escherichia coli penicillin-binding protein 5 and purification by dye chromatography. Eur. J. Biochem. 204 197-202 PubMed GONUTS page
↑ Spratt, BG (1977) Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur. J. Biochem. 72 341-52 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Matsuhashi, M et al. (1978) Isolation of a mutant of Escherichia coli lacking penicillin-sensitive D-alanine carboxypeptidase IA. Proc. Natl. Acad. Sci. U.S.A. 75 2631-5 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Amanuma, H & Strominger, JL (1980) Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes. J. Biol. Chem. 255 11173-80 PubMed GONUTS page
↑ Hesek, D et al. (2004) Synthetic peptidoglycan substrates for penicillin-binding protein 5 of Gram-negative bacteria. J. Org. Chem. 69 778-84 PubMed GONUTS page
↑ Henderson, TA et al. (1997) AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J. Bacteriol. 179 6112-21 PubMed GONUTS page

[PMID:17685588-1] 1.0 ^1.1 Zhang, W et al. (2007) Catalytic mechanism of penicillin-binding protein 5 of Escherichia coli. Biochemistry 46 10113-21 PubMed GONUTS page

[PMID:21873635-2] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:368033-3] Matsuhashi, M et al. (1979) Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity. J. Bacteriol. 137 644-7 PubMed GONUTS page

[PMID:10692378-4] Nelson, DE & Young, KD (2000) Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli. J. Bacteriol. 182 1714-21 PubMed GONUTS page

[PMID:1740130-5] van der Linden, MP et al. (1992) Cytoplasmic high-level expression of a soluble, enzymatically active form of the Escherichia coli penicillin-binding protein 5 and purification by dye chromatography. Eur. J. Biochem. 204 197-202 PubMed GONUTS page

[PMID:319999-6] Spratt, BG (1977) Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur. J. Biochem. 72 341-52 PubMed GONUTS page

[PMID:351612-7] 7.0 ^7.1 ^7.2 Matsuhashi, M et al. (1978) Isolation of a mutant of Escherichia coli lacking penicillin-sensitive D-alanine carboxypeptidase IA. Proc. Natl. Acad. Sci. U.S.A. 75 2631-5 PubMed GONUTS page

[PMID:7002918-8] 8.0 ^8.1 ^8.2 ^8.3 Amanuma, H & Strominger, JL (1980) Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes. J. Biol. Chem. 255 11173-80 PubMed GONUTS page

[PMID:14750804-9] Hesek, D et al. (2004) Synthetic peptidoglycan substrates for penicillin-binding protein 5 of Gram-negative bacteria. J. Org. Chem. 69 778-84 PubMed GONUTS page

[PMID:9324260-10] Henderson, TA et al. (1997) AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J. Bacteriol. 179 6112-21 PubMed GONUTS page

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ECOLI:DACA

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