ECOLI:DPS

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dps (synonyms: pexB, vtm)
Protein Name(s)	DNA protection during starvation protein
External Links
UniProt	P0ABT2
EMBL	X69337 U04242 U00096 AP009048 X14180
PIR	A46401
RefSeq	NP_415333.1 YP_489085.1
PDB	1DPS 1F30 1F33 1JRE 1JTS 1L8H 1L8I 2W9R 3O2H
PDBsum	1DPS 1F30 1F33 1JRE 1JTS 1L8H 1L8I 2W9R 3O2H
ProteinModelPortal	P0ABT2
SMR	P0ABT2
DIP	DIP-35919N
IntAct	P0ABT2
MINT	MINT-1220368
STRING	511145.b0812
PhosSite	P0809382
SWISS-2DPAGE	P0ABT2
PaxDb	P0ABT2
PRIDE	P0ABT2
EnsemblBacteria	AAC73899 BAA35484
GeneID	12930979 945101
KEGG	ecj:Y75_p0785 eco:b0812
PATRIC	32116827
EchoBASE	EB1387
EcoGene	EG11415
eggNOG	COG0783
HOGENOM	HOG000273542
InParanoid	P0ABT2
KO	K04047
OMA	DHQDTIA
OrthoDB	EOG6Z9B6G
PhylomeDB	P0ABT2
BioCyc	EcoCyc:EG11415-MONOMER ECOL316407:JW0797-MONOMER
EvolutionaryTrace	P0ABT2
PRO	PR:P0ABT2
Proteomes	UP000000318 UP000000625
Genevestigator	P0ABT2
GO	GO:0005737 GO:0016020 GO:0009295 GO:0003677 GO:0008199 GO:0016722 GO:0006879 GO:0030261 GO:0042594
Gene3D	1.20.1260.10
HAMAP	MF_01441
InterPro	IPR002177 IPR023188 IPR023067 IPR009078 IPR012347 IPR008331
Pfam	PF00210
PIRSF	PIRSF005900
PRINTS	PR01346
SUPFAM	SSF47240
PROSITE	PS00818 PS00819

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0016020	membrane	PMID:16858726^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9546221^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ABT2	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ABT2	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:10551881^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9546221^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ABT2	F	Seeded From UniProt	complete
involved_in	GO:0042594	response to starvation	PMID:1340475^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	PMID:12163499^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:1340475^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008331	P	Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008331	F	Seeded From UniProt	complete
enables	GO:0016722	oxidoreductase activity, oxidizing metal ions	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023067 InterPro:IPR023188	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023067 InterPro:IPR023188	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000078115	F	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000078115	F	Seeded From UniProt	complete
enables	GO:0008199	ferric iron binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000078115	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000078115	C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
involved_in	GO:0030261	chromosome condensation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0226	P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0006879	cellular iron ion homeostasis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0409	P	Seeded From UniProt	complete
part_of	GO:0009295	nucleoid	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0187	C	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ ^2.0 ^2.1 Grant, RA et al. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol. 5 294-303 PubMed GONUTS page
↑ Azam, TA & Ishihama, A (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274 33105-13 PubMed GONUTS page
↑ ^4.0 ^4.1 Almirón, M et al. (1992) A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6 2646-54 PubMed GONUTS page
↑ Ilari, A et al. (2002) Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J. Biol. Chem. 277 37619-23 PubMed GONUTS page

[PMID:16858726-1] 1.0 ^1.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:9546221-2] 2.0 ^2.1 Grant, RA et al. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol. 5 294-303 PubMed GONUTS page

[PMID:10551881-3] Azam, TA & Ishihama, A (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274 33105-13 PubMed GONUTS page

[PMID:1340475-4] 4.0 ^4.1 Almirón, M et al. (1992) A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev. 6 2646-54 PubMed GONUTS page

[PMID:12163499-5] Ilari, A et al. (2002) Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J. Biol. Chem. 277 37619-23 PubMed GONUTS page

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ECOLI:DPS

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