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ECOBD:C6EJZ8

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Species (Taxon ID) Escherichia coli (strain B / BL21-DE3). (469008)
Gene Name(s) clpB (ECO:0000313 with EMBL:ACT44301.1)
Protein Name(s) ATP-dependent chaperone ClpB (ECO:0000313 with EMBL:ACT28158.1)

ClpB chaperone (ECO:0000313 with EMBL:CAQ32963.1) Protein disaggregation chaperone (ECO:0000313 with EMBL:ACT44301.1)

External Links
UniProt C6EJZ8
EMBL CP001665
CP001509
AM946981
RefSeq YP_003000219.1
YP_003035343.1
YP_003055072.1
ProteinModelPortal C6EJZ8
SMR C6EJZ8
STRING 469008.ECBD_1092
EnsemblBacteria ACT28158
ACT44301
CAQ32963
GeneID 8115944
8159536
8182681
KEGG ebd:ECBD_1092
ebe:B21_02446
ebl:ECD_02482
eggNOG COG0542
HOGENOM HOG000218211
KO K03695
OMA PLRRLMQ
Proteomes UP000001509
UP000002032
UP000009074
GO GO:0005737
GO:0005524
GO:0016485
GO:0009408
Gene3D 1.10.1780.10
3.40.50.300
InterPro IPR003593
IPR003959
IPR017730
IPR019489
IPR004176
IPR001270
IPR018368
IPR028299
IPR023150
IPR027417
Pfam PF00004
PF07724
PF02861
PF10431
PRINTS PR00300
SMART SM00382
SM01086
SUPFAM SSF52540
TIGRFAMs TIGR03346
PROSITE PS00870
PS00871

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0019538

protein metabolic process

PMID:10982797[1]

ECO:0000315

P

Fig. 6 illustrates the amount of ATP hydrolysis by clpB mutants and wild types.

complete
CACAO 9611

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001270
InterPro:IPR003959
InterPro:IPR018368

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017730

C

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017730

P

Seeded From UniProt

complete

involved_in

GO:0019538

protein metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR036628

P

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017730

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000040

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000143756

F

Seeded From UniProt

complete

involved_in

GO:0019538

protein metabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000143756

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000143756

C

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000143756

P

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000143756

P

Seeded From UniProt

complete

Notes

References

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

  1. Barnett, ME et al. (2000) Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. J. Biol. Chem. 275 37565-71 PubMed GONUTS page