Detail Information for IndEnz0002016944
IED ID IndEnz0002016944
Enzyme Type ID protease016944
Protein Name Chaperone protein ClpC, chloroplastic
ATP-dependent Clp protease ATP-binding subunit ClpC homolog
Casein lytic proteinase C
Gene Name
Organism Pisum sativum (Garden pea)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Fabeae Pisum Pisum sativum (Garden pea)
Enzyme Sequence MARVLAQSLSVPGLVAGHKDSQHKGSGKSKRSVKTMCALRTSGLRMSGFSGLRTFNHLNTMMRPGLDFHSKVSKAVSSRRARAKRFIPRAMFERFTEKAIKVIMLAQEEARRLGHNFVGTEQILLGLIGEGTGIAAKVLKSMGINLKDARVEVEKIIGRGSGFVAVEIPFTPRAKRVLELSQEEARQLGHNYIGSEHLLLGLLREGEGVAARVLENLGADPTNIRTQVIRMVGESADSVTATVGSGSSNNKTPTLEEYGTNLTKLAEEGKLDPVVGRQPQIERVTQILGRRTKNNPCLIGEPGVGKTAIAEGLAQRIANGDVPETIEGKKVITLDMGLLVAGTKYRGEFEERLKKLMEEIKQSDDIILFIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRKHIEKDPDLERRFQPVKVPEPTVDETIQILKGLRERYEIHHKLRYTDEALIAAAQLSYQYISDRFLPDKAIDLVDEAGSRVRLQHAQLPEEAKELDKEVRKIVKEKEEYVRNQDFEKAGELRDKEMDLKAQISALIEKGKEMSKAETETADEGPIVTEVDIQHIVSSWTGIPVDKVSADESDRLLKMEDTLHKRIIGQDEAVQAISRAIRRARVGLKNPNRPIASFIFSGPTGVGKSELAKALAAYYFGSEEAMIRLDMSEFMERHTVSKLIGSPPGYVGYTEGGQLTEAVRRRPYTVVLFDEIEKAHPDVFNMMLQILEDGRLTDSKGRTVDFKNTLLIMTSNVGSSVIEKGGRRIGFDLDYDEKDSSYNRIKSLVTEELKQYFRPEFLNRLDEMIVFRQLTKLEVKEIADIMLKEVFQRLKTKEIELQVTERFRDRVVDEGYNPSYGARPLRRAIMRLLEDSMAEKMLAREIKEGDSVIVDVDSDGKVIVLNGSSGTPESLPEALSI
Enzyme Length 922
Uniprot Accession Number P35100
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Molecular chaperone that may interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast. {ECO:0000269|PubMed:1735703}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 300..307; /note=ATP; /evidence=ECO:0000250; NP_BIND 643..650; /note=ATP; /evidence=ECO:0000250
Features Chain (1); Domain (2); Nucleotide binding (2); Region (4); Transit peptide (1)
Keywords ATP-binding;Chaperone;Chloroplast;Nucleotide-binding;Plastid;Repeat;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 9405363;
Motif
Gene Encoded By
Mass 102,711
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda