Detail Information for IndEnz0002004539
IED ID IndEnz0002004539
Enzyme Type ID protease004539
Protein Name RNA helicase CrhR
EC 3.6.4.13
Gene Name crhR deaD slr0083
Organism Synechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Merismopediaceae Synechocystis unclassified Synechocystis Synechocystis sp. PCC 6803 Synechocystis sp. (strain PCC 6803 / Kazusa)
Enzyme Sequence MTNTLTSTFADLGLSEKRCQLLADIGFEAPTQIQTEAIPLLLSGRDMLAQSQTGTGKTAAFALPLMDRIDPEGDLQALILTPTRELAQQVAEAMKDFSHERRLFILNVYGGQSIERQIRSLERGVQIVVGTPGRVIDLIDRKKLKLETIQWVVLDEADEMLSMGFIDDVKTILRKTPPTRQTACFSATMPREIKELVNQFLNDPALVTVKQTQSTPTRIEQQLYHVPRGWSKAKALQPILEMEDPESAIIFVRTKQTAADLTSRLQEAGHSVDEYHGNLSQSQRERLVHRFRDGKIKLVVATDIAARGLDVNNLSHVVNFDLPDNAETYIHRIGRTGRAGKTGKAIALVEPIDRRLLRSIENRLKQQIEVCTIPNRSQVEAKRIEKLQEQLKEALTGERMASFLPLVRELSDEYDAQAIAAAALQMIYDQSCPHWMKSDWEVPEVDFNKPVLRRGRNAGGGQNKSGGGYQGKPGKPRRSSGGRRPAYSDRQQ
Enzyme Length 492
Uniprot Accession Number Q55804
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Helicase inhibited by the slowly-hydrolyzing ATP analog ATP-gamma-S (PubMed:15542859). Protein is rapidly degraded upon shifting from 20 to 30 degrees Celsius, the degradation machinery is only transiently present in cells grown at 30 degrees Celsius, is inhibited by commercial protease inhibitors and requires full-length protein expression (the N-terminal fragment does not induce proteolysis although it can be degraded by widl-type extract) (PubMed:24509313). {ECO:0000269|PubMed:15542859, ECO:0000269|PubMed:24509313}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:15542859};
DNA Binding
EC Number 3.6.4.13
Enzyme Function FUNCTION: An ATP-dependent bidirectional RNA helicase with RNA-dependent ATPase activity; does not unwind dsDNA, uses only (d)ATP (PubMed:15542859). Also has ATP-dependent RNA annealing activity; concurrent annealing and helicase activity promote strand-exchange activity (PubMed:15542859). In vitro has low helicase processivity, annealing processivity is probably higher (PubMed:15542859). Required for correct cold adaptation, probably by aiding translation of mRNAs required for photosynthesis and electron transport (PubMed:22575444). Probably regulates the cold-shock-inducible expression of the GroESL chaperones (PubMed:19926653). May partially regulate its own expression at both the transcriptional and post-transcriptional level (experiments used a construct expressing a 25 kDa trunacted protein which might have dominant-negative effects); is probably not directly involved in the pathway responsible for mRNA degradation (PubMed:23119089). {ECO:0000269|PubMed:15542859, ECO:0000269|PubMed:19926653, ECO:0000269|PubMed:22575444, ECO:0000305|PubMed:23119089}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 51..58; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541
Features Chain (1); Domain (2); Motif (2); Nucleotide binding (1); Region (1)
Keywords ATP-binding;Cell inner membrane;Cell membrane;Cytoplasm;Helicase;Hydrolase;Membrane;Nucleotide-binding;Reference proteome;Stress response;Thylakoid
Interact With
Induction INDUCTION: Constitutively expressed; higher levels are found in light-grown cells and lower levels in dark cells unless grown in glucose (at protein level) (PubMed:11027719, PubMed:23119089). Transcript level is regulated by the redox state of the plastoquinone pool; transcript accumulates when electrons flow between PSII and cytochrome b6-f complex (reduction of the electron transport chain) (PubMed:11027719). LexA-like repressor probably represses its expression at least in part (PubMed:16840531). Induced by cold with maximal RNA induction at 15 degrees Celsius and maximal protein induction at 15-20 degrees Celsius (at protein level) (PubMed:23119089). Also expressed as part of the rimO-chrR operon; expression is greater at 20 than 30 degrees Celsius. The rimO-crhR transcript is processed between the 2 genes by RNase E (rne) (PubMed:32209657). {ECO:0000269|PubMed:11027719, ECO:0000269|PubMed:16840531, ECO:0000269|PubMed:23119089, ECO:0000269|PubMed:32209657}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19926653, ECO:0000269|PubMed:22368073, ECO:0000269|PubMed:23119089, ECO:0000269|PubMed:27215789}. Cell inner membrane {ECO:0000305|PubMed:27215789}; Peripheral membrane protein {ECO:0000305}. Cellular thylakoid membrane {ECO:0000269|PubMed:27215789}; Peripheral membrane protein {ECO:0000305}. Note=A small amount is localized to the cell inner membrane and the thylakoid membrane, and cosediments with polysomes. {ECO:0000269|PubMed:27215789}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 18000013;
Motif MOTIF 7..35; /note=Q motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU00552; MOTIF 155..158; /note=DEAD box; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541
Gene Encoded By
Mass 55,120
Kinetics
Metal Binding
Rhea ID RHEA:13065
Cross Reference Brenda