Text mining Term | acylase |
---|---|
UniProt ID | QUIP_PSEPK |
Name |
Acyl-homoserine lactone acylase quiP AHL acylase quiP Acyl-HSL acylase quiP Acyl-homoserine lactone acylase quiP subunit alpha Acyl-homoserine lactone acylase quiP subunit beta Acyl-HSL acylase quiP subunit alpha Acyl-HSL acylase quiP subunit beta |
Gene Names |
quiP
|
Taxonomy | Pseudomonas putida KT2440 |
Function |
Catalyzes the deacylation of acyl-homoserine lactone (AHL or acyl-HSL), releasing homoserine lactone (HSL) and the corresponding fatty acid. Possesses a specificity for the degradation of long-chain acyl-HSLs (side chains of seven or more carbons in length) (By similarity). |
---|---|
Subcellular location |
Periplasm (Potential). |
GO:0017000 | antibiotic biosynthetic process | BP |
GO:0009372 | quorum sensing | BP |
GO:0016811 | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | MF |
GO:0042597 | periplasmic space | CC |
>gi|26987844|ref|NP_743269.1| acylase [Pseudomonas putida KT2440] MAAPAFPPFRLRFATAATLLGMLGLAGCQTGGYQDSVPPTSGVQPLKGLAQNVSVRRNAMGAPLIESSSF HDALFSLGYVHAGDRIEQMVAMRLLAQGRLAELAGSEALDIDRLMRAANLKQSAAQQYADASPRLKRFFE VYARGVNAYLFRYRDKLPAGLASSGYRPEYWKPEDSALIFCLYAFSQSVNLQEELSALTLAQKAGSDKLA WLLPGAPDEPLAEMEVDKLKGLNLASQLPGLPALAAASQKLADLDLLGSPGSANLALGPQRSRSGKSLLA SDSRAAWALSPVQINTSKYQVAGLSLPGLPIVLAGYNGKLAWSSSAVMADNQDLFLEQLRRQGSQLSYLA DGKWLPARARSETYFVRGQRPVREVMYDTRHGTLLAQPENASLGLALNLPQFKGDRSLDALFDLTRAKNV ERAFDSTREVTAAAVNFVFAEPEHIGWQVSGRYPNRREGQGLLPSPGWDGRYDWDGYADPMLHPYDQDPP AGWIGHANQRSLPRGYGMQLSSTWYYPERAERLAQLAGNGRHDSRSLMALQNDQVTLLANKLKQMFDAPG MAQPLKQAIDALPAGQRDKARDTLARLKAFDGRLSPVSADAALYELFLQEVARQTFLDDLGPESGPAWQA FVGNARLSFSAQADHLLGRDDSPFWDDRNTPQKEDKPAILARSLAGAMEAGIAQLGADRRTWQWGKLHQY RWPAPAYHGLGDAISRSPLAAGGDFTTLALTPFAWGSDFDTHLPASARMIVDFGQAEPLQILTSSGQSGN PASAHYRDGLDAWFKGRFMSLPLQQQNFGRAYGNQRLTLVPGR |
Ensembl Gene | |
---|---|
UniGene | |
PDB | |
RefSeq |
NP_743269.1 |
Pfam |
PF01804 |