| IED ID |
IndEnz0002016800 |
| Enzyme Type ID |
protease016800 |
| Protein Name |
ATP-dependent Clp protease ATP-binding subunit ClpA
|
| Gene Name |
clpA c1019 |
| Organism |
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Enterobacteriaceae
Escherichia
Escherichia coli
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
|
| Enzyme Sequence |
MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQRVLQRAVFHVQSSGRNEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPTQSSDPGSQPNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAEAAH |
| Enzyme Length |
758 |
| Uniprot Accession Number |
P0ABI0 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
|
| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| Enzyme Function |
FUNCTION: ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins (By similarity). {ECO:0000250}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
NP_BIND 214..221; /note=ATP; /evidence=ECO:0000255; NP_BIND 495..502; /note=ATP; /evidence=ECO:0000255 |
| Features |
Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Nucleotide binding (2); Region (5) |
| Keywords |
ATP-binding;Chaperone;Nucleotide-binding;Repeat |
| Interact With |
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| Induction |
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| Subcellular Location |
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| Modified Residue |
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| Post Translational Modification |
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| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
84,207 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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