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ECO27:B7UJR0
Contents
Species (Taxon ID) | Escherichia coli O127:H6 (strain E2348/69 / EPEC). (574521) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | ATP-dependent Clp protease proteolytic subunit (ECO:0000256 with HAMAP-Rule:MF_00444, ECO:0000256 with RuleBase:RU003567)
Endopeptidase Clp (ECO:0000256 with HAMAP-Rule:MF_00444) | |
External Links | ||
UniProt | B7UJR0 | |
EMBL | FM180568 | |
RefSeq | YP_002327949.1 | |
ProteinModelPortal | B7UJR0 | |
SMR | B7UJR0 | |
STRING | 574521.E2348C_0372 | |
PRIDE | B7UJR0 | |
EnsemblBacteria | CAS07920 | |
GeneID | 7061803 | |
KEGG | ecg:E2348C_0372 | |
PATRIC | 18339710 | |
eggNOG | COG0740 | |
HOGENOM | HOG000285833 | |
KO | K01358 | |
OMA | ARMNELM | |
OrthoDB | EOG6Z3KQ0 | |
BioCyc | ECOL574521:GJAO-384-MONOMER | |
Proteomes | UP000008205 | |
GO | GO:0005737 GO:0004252 | |
Gene3D | 3.90.226.10 | |
HAMAP | MF_00444 | |
InterPro | IPR001907 IPR029045 IPR023562 IPR018215 | |
PANTHER | PTHR10381 | |
Pfam | PF00574 | |
PRINTS | PR00127 | |
SUPFAM | SSF52096 | |
TIGRFAMs | TIGR00493 | |
PROSITE | PS00382 PS00381 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:1901800 |
positive regulation of proteasomal protein catabolic process |
ECO:0000314 |
P |
Figure 6 - With ClpP in complex with ClpX, slippage of the protein occurs much less and thus the ClpP works to positively regulate the catabolic process of GFP. |
complete | |||||
GO:0010498 |
proteasomal protein catabolic process |
ECO:0000314 |
P |
Figure 4 - ClpP works with ClpA and ClpX in vitro to degrate SsrA-tagged proteins. |
complete | |||||
enables |
GO:0004252 |
serine-type endopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
GO:1901800 |
positive regulation of proteasomal protein catabolic process |
ECO:0000315 |
P |
Figure 5 shows ClpP- strains degrade the SsrA-tagged proteins more slowly than wild type strain, in vivo. |
complete | |||||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008233 |
peptidase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008236 |
serine-type peptidase activity |
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 | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000089051 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004252 |
serine-type endopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000089051 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000089051 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Maillard, RA et al. (2011) ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell 145 459-69 PubMed GONUTS page
- ↑ 2.0 2.1 Gottesman, S et al. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12 1338-47 PubMed GONUTS page