| Text mining Term | acylase |
|---|---|
| UniProt ID | QUIP_PSEPK |
| Name |
Acyl-HSL acylase quiP AHL acylase quiP Acyl-homoserine lactone acylase quiP subunit alpha Acyl-HSL acylase quiP subunit alpha Acyl-homoserine lactone acylase quiP Acyl-HSL acylase quiP subunit beta Acyl-homoserine lactone 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 |