Detail Information for IndEnz0002018012
IED ID IndEnz0002018012
Enzyme Type ID protease018012
Protein Name ATP-dependent Clp protease ATP-binding subunit ClpX
Gene Name clpX SPP_1592
Organism Streptococcus pneumoniae (strain P1031)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae Streptococcus pneumoniae (strain P1031)
Enzyme Sequence MSTNRKNDMMVYCSFCGKNQEEVQKIIAGNNAFICNECVELAQEIIREELVEEVLADLSEVPKPIELLHILNHYVIGQDRAKRALAVAVYNHYKRINFHDTREESEDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATALTEAGYVGEDVENILLKLLQVADFNIERAERGIIYVDEIDKIAKKSENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPQQEMIQVDTKNILFIVGGAFDGIEEIVKQRLGEKVIGFGQNNKAIDENSSYMQEIIAEDIQKFGIIPELIGRLPVFAALEQLTVDDLVRILKEPRNALVKQYQTLLSYDDVELEFDDEALQEIANKAIERKTGARGLRSIIEETMLDVMFEVPSQENVKLVRITKETVDGTDKPILETA
Enzyme Length 410
Uniprot Accession Number C1CLR8
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 120..127; /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 45,798
Kinetics
Metal Binding METAL 13; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 16; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 35; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 38; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250
Rhea ID
Cross Reference Brenda