| IED ID |
IndEnz0002016801 |
| Enzyme Type ID |
protease016801 |
| Protein Name |
ATP-dependent Clp protease ATP-binding subunit ClpA
|
| Gene Name |
clpA lopD b0882 JW0866 |
| Organism |
Escherichia coli (strain K12) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Enterobacteriaceae
Escherichia
Escherichia coli
Escherichia coli (strain K12)
|
| Enzyme Sequence |
MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQRVLQRAVFHVQSSGRNEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPTQSSDPGSQPNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAEAAH |
| Enzyme Length |
758 |
| Uniprot Accession Number |
P0ABH9 |
| Absorption |
|
| Active Site |
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| Activity Regulation |
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| Binding Site |
|
| 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. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
NP_BIND 214..221; /note=ATP; /evidence=ECO:0000255; NP_BIND 495..502; /note=ATP; /evidence=ECO:0000255 |
| Features |
Beta strand (31); Chain (1); Compositional bias (1); Domain (1); Helix (36); Nucleotide binding (2); Region (5); Sequence conflict (3); Turn (7) |
| Keywords |
3D-structure;ATP-binding;Chaperone;Direct protein sequencing;Nucleotide-binding;Reference proteome;Repeat |
| Interact With |
P0AEC5; P0A6G7; P0A8Q6; P68646 |
| 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 |
Electron microscopy (10); X-ray crystallography (11) |
| Cross Reference PDB |
1K6K;
1KSF;
1LZW;
1MBU;
1MBV;
1MBX;
1MG9;
1R6B;
1R6C;
1R6O;
1R6Q;
5OFO;
5OG1;
6UQE;
6UQO;
6W1Z;
6W20;
6W21;
6W22;
6W23;
6W24;
|
| Mapped Pubmed ID |
15037248;
15690043;
16606699;
1783205;
19317833;
24561554;
24627523;
28798962;
32313240;
|
| 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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