IED ID |
IndEnz0002014128 |
Enzyme Type ID |
protease014128 |
Protein Name |
ATP-dependent protease ATP-binding subunit-like protein
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Gene Name |
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Organism |
Rhodococcus erythropolis (Arthrobacter picolinophilus) |
Taxonomic Lineage |
cellular organisms
Bacteria
Terrabacteria group
Actinobacteria
Actinomycetia (high G+C Gram-positive bacteria)
Corynebacteriales
Nocardiaceae
Rhodococcus
Rhodococcus erythropolis group
Rhodococcus erythropolis (Arthrobacter picolinophilus)
|
Enzyme Sequence |
MPYITDMLRDRNSAATPPAEERSEPVPVGAFDARRLSKALSSKIVGQQAAVDAVVRAISIAHVGATDPTRPLANILLVGPTGVGKTELVRRVAAELRSGPDDLCRIDMNALAQEHYAASFSGAPPGYAGSKESFTLFDKNTVEGDPYTPGIVLFDEVEKADPTVLRALLQVLDNGELRLANGQQKISFRNSYVFLTSNLGSAAVAERRRSHLRQLADRVRIDRPRHGHHLVQRALEKFFDPEFFNRIDETVILDEFDDQTAEQVTRLEIELITTRLARRGIDVEVDDSAVALLQRRGFDPVYGARGLRRTIRNVLADPVAGAVLDLRPVGTQPLALQARAVGDQIQVKKAP |
Enzyme Length |
351 |
Uniprot Accession Number |
Q01357 |
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 |
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catalytic Activity |
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DNA Binding |
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EC Number |
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Enzyme Function |
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Temperature Dependency |
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PH Dependency |
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Pathway |
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nucleotide Binding |
NP_BIND 79..86; /note=ATP; /evidence=ECO:0000250 |
Features |
Chain (1); Nucleotide binding (1); Region (1) |
Keywords |
ATP-binding;Chaperone;Nucleotide-binding |
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 |
38,510 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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