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ECOLI:CLPA

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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

PMID:9573050[1]

ECO:0000314

F

Figure 4 - ClpA complexes with ClpP to degrade SsrA-tagged protein, in vitro.

complete
CACAO 9061

enables

GO:0004176

ATP-dependent peptidase activity

PMID:9573050[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043335

protein unfolding

PMID:19726681[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:3049606[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:24580753[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:7961938[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:24362308[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000108

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

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

enables

GO:0016887

ATPase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013461

F

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:0043335

protein unfolding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013461

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

Notes

References

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

  1. 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
  2. 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
  3. 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
  4. Krisko, A et al. (2014) Inferring gene function from evolutionary change in signatures of translation efficiency. Genome Biol. 15 R44 PubMed GONUTS page
  5. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  6. 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
  7. 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