Detail Information for IndEnz0002017694
IED ID IndEnz0002017694
Enzyme Type ID protease017694
Protein Name ATP-dependent Clp protease ATP-binding subunit ClpX
Gene Name clpX AM310
Organism Anaplasma marginale (strain St. Maries)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rickettsiales Anaplasmataceae Anaplasma Anaplasma marginale Anaplasma marginale (strain St. Maries)
Enzyme Sequence MSEARKGAYSCSFCGKLHSEVRKLIAGPRVYICNECVELCSGILQEEGRPARQGGFDLKPPEIKQVLDEYVIGQEHSKKVLSVAVYNHYKRLRNSGVISEVEISKSNVLLIGPTGSGKTLLARTLARVLQVPFAMADATTLTEAGYVGEDVENILLKLLQAANFNVEAAQRGIIYIDEVDKISRKSENASITRDVSGEGVQQALLKVIEGTVSSVPPQGGRKHPHQEFIQINTDNILFIFGGAFDGLEKIIEARNRGSCMGFEANVQKIADKRKDILCYTEPEDLVKFGLIPEFVGRIPVVTSLGRLDEETLYRILVEPKNSLVKQYTKLFEMDNLELKFDNAALLAVAKKAVARNTGARGLRAIMESLLLDFMFNPLGCEGGKVVVDAAMVEDVMMSRNCFESG
Enzyme Length 405
Uniprot Accession Number Q5PBC9
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 113..120; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00175
Features Chain (1); Domain (1); Metal binding (4); Nucleotide binding (1)
Keywords ATP-binding;Chaperone;Metal-binding;Nucleotide-binding;Zinc
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 44,562
Kinetics
Metal Binding METAL 11; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 14; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 33; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 36; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250
Rhea ID
Cross Reference Brenda