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ECOBD:C6EJZ8
Contents
| 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 |
ECO:0000315 |
P |
Fig. 6 illustrates the amount of ATP hydrolysis by clpB mutants and wild types. |
complete | |||||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009408 |
response to heat |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0019538 |
protein metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0042026 |
protein refolding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
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 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000143756 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005737 |
cytoplasm |
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 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000143756 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0042026 |
protein refolding |
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.
- ↑ 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