Detail Information for IndEnz0002011414
IED ID IndEnz0002011414
Enzyme Type ID protease011414
Protein Name Uncharacterized ABC transporter ATP-binding protein YwjA
Gene Name ywjA BSU37230
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MLRQFFSYYKPYKTLFFLDFFSAIAGGLMELSFPLIVNYFIDTLLPGRDWGLIIATSIGLFAVYALSSALQYIVTYWGHMLGINIETDMRKSLFDHLQKLSFKFYDNNKTGTLMSKLTNDLMYIGEVAHHGPEDLFIAVMTILGAFGVMLFINWQLALLTFIIMPIVIWLALYFNKKMTKAFTTLNKDIGDFSARVENNIGGIRLVQAFGNEAFEKERFAVNNQRFRVTKLSSYKIMAKNGSISYMLTRFVTLFVLLCGTWFVIRGSLSYGEFVAFVLLTNVLFRPIDKINAIIEMYPRGIAGFKSYMELMETEPDIQDSPDSKDVSGLKGNIRYKHVSFGYDDHHNVLNDINLSIQAGETVAFVGPSGAGKSTLCSLLPRFYEASEGDITIDGISIKDMTLSSLRGQIGVVQQDVFLFSGTLRENIAYGRLGASEEDIWQAVKQAHLEELVHNMPDGLDTMIGERGVKLSGGQKQRLSIARMFLKNPSILILDEATSALDTETEAAIQKALQELSEGRTTLVIAHRLATIKDADRIVVVTNNGIEEQGRHQDLIEAGGLYSRLHQAQFGQMVHR
Enzyme Length 575
Uniprot Accession Number P45861
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 366..373; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00434
Features Chain (1); Domain (2); Nucleotide binding (1); Transmembrane (6)
Keywords ATP-binding;Cell membrane;Membrane;Nucleotide-binding;Reference proteome;Transmembrane;Transmembrane helix;Transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}; Multi-pass membrane protein {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 64,563
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda