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ECOLI:CLPA
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | clpA (synonyms: lopD) | |
Protein Name(s) | ATP-dependent Clp protease ATP-binding subunit ClpA | |
External Links | ||
UniProt | P0ABH9 | |
EMBL | M31045 U00096 AP009048 M23220 | |
PIR | B64827 | |
RefSeq | NP_415403.1 YP_489155.1 | |
PDB | 1K6K 1KSF 1LZW 1MBU 1MBV 1MBX 1MG9 1R6B 1R6C 1R6O 1R6Q | |
PDBsum | 1K6K 1KSF 1LZW 1MBU 1MBV 1MBX 1MG9 1R6B 1R6C 1R6O 1R6Q | |
ProteinModelPortal | P0ABH9 | |
SMR | P0ABH9 | |
BioGrid | 850131 | |
DIP | DIP-35409N | |
IntAct | P0ABH9 | |
STRING | 511145.b0882 | |
PaxDb | P0ABH9 | |
PRIDE | P0ABH9 | |
EnsemblBacteria | AAC73969 BAA35601 | |
GeneID | 12932326 945764 | |
KEGG | ecj:Y75_p0855 eco:b0882 | |
PATRIC | 32116973 | |
EchoBASE | EB0154 | |
EcoGene | EG10156 | |
eggNOG | COG0542 | |
HOGENOM | HOG000218210 | |
InParanoid | P0ABH9 | |
KO | K03694 | |
OMA | FTHQDHS | |
OrthoDB | EOG65F8SM | |
PhylomeDB | P0ABH9 | |
BioCyc | EcoCyc:EG10156-MONOMER ECOL316407:JW0866-MONOMER MetaCyc:EG10156-MONOMER | |
SABIO-RK | P0ABH9 | |
EvolutionaryTrace | P0ABH9 | |
PRO | PR:P0ABH9 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P0ABH9 | |
GO | GO:0005524 GO:0004176 GO:0006508 GO:0006979 | |
Gene3D | 1.10.1780.10 3.40.50.300 | |
InterPro | IPR003593 IPR003959 IPR019489 IPR004176 IPR013461 IPR001270 IPR018368 IPR028299 IPR023150 IPR027417 | |
PANTHER | PTHR11638:SF14 | |
Pfam | PF00004 PF07724 PF02861 PF10431 | |
PRINTS | PR00300 | |
SMART | SM00382 SM01086 | |
SUPFAM | SSF52540 | |
TIGRFAMs | TIGR02639 | |
PROSITE | PS00870 PS00871 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004176 |
ATP-dependent peptidase activity |
ECO:0000314 |
F |
Figure 4 - ClpA complexes with ClpP to degrade SsrA-tagged protein, in vitro. |
complete | |||||
enables |
GO:0004176 |
ATP-dependent peptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0043335 |
protein unfolding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016887 |
ATPase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006979 |
response to oxidative stress |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0005524 |
ATP binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005524 |
ATP binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004176 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016887 |
ATPase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
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:0043335 |
protein unfolding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 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
- ↑ Kress, W et al. (2009) Both ATPase domains of ClpA are critical for processing of stable protein structures. J. Biol. Chem. 284 31441-52 PubMed GONUTS page
- ↑ Katayama, Y et al. (1988) The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J. Biol. Chem. 263 15226-36 PubMed GONUTS page
- ↑ Krisko, A et al. (2014) Inferring gene function from evolutionary change in signatures of translation efficiency. Genome Biol. 15 R44 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Singh, SK & Maurizi, MR (1994) Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli. J. Biol. Chem. 269 29537-45 PubMed GONUTS page
- ↑ Miller, JM & Lucius, AL (2014) ATPγS competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation. Biophys. Chem. 185 58-69 PubMed GONUTS page