ID K0XMU9_PSEAI Unreviewed; 290 AA. AC K0XMU9; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 11-DEC-2013, entry version 7. DE RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme; DE EC=2.1.1.-; DE EC=3.4.23.43; GN ORFNames=A161_22513; OS Pseudomonas aeruginosa PAO579. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1191475; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PAO579; RX PubMed=23144378; DOI=10.1128/JB.01406-12; RA Withers T.R., Johnson S.L., Yu H.D.; RT "Draft Genome Sequence for Pseudomonas aeruginosa Strain PAO579, a RT Mucoid Derivative of PAO381."; RL J. Bacteriol. 194:6617-6617(2012). CC -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates CC the N-terminal (generally Phe) residue (By similarity). CC -!- CATALYTIC ACTIVITY: Typically cleaves a -Gly-|-Phe- bond to CC release an N-terminal, basic peptide of 5-8 residues from type IV CC prepilin, and then N-methylates the new N-terminal amino group, CC the methyl donor being S-adenosyl-L-methionine. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By CC similarity). CC -!- SIMILARITY: Belongs to the peptidase A24 family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ALOF01000015; EJZ72418.1; -; Genomic_DNA. DR ProteinModelPortal; K0XMU9; -. DR EnsemblBacteria; EJZ72418; EJZ72418; A161_22513. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR InterPro; IPR010627; Pept_A24A_N. DR InterPro; IPR014032; Peptidase_A24A_bac. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR Pfam; PF06750; DiS_P_DiS; 1. DR Pfam; PF01478; Peptidase_A24; 1. DR PRINTS; PR00864; PREPILNPTASE. PE 3: Inferred from homology; KW Hydrolase; Membrane; Methyltransferase; Multifunctional enzyme; KW Protease; Transferase; Transmembrane. SQ SEQUENCE 290 AA; 31870 MW; 57A8526EB18FB752 CRC64; MPLLDYLASH PLAFVLCTIL LGLLVGSFLN VVVHRLPKMM ERNWKAEARE ALGLEPEPKQ ATYNLVLPNS ACPRCGHEIR PWENIPLVSY LALGGKCSSC KAAIGKRYPL VELATALLSG YVAWHFGFTW QAGAMLLLTW GLLAMSLIDA DHQLLPDVLV LPLLWLGLIA NHFGLFASLD DALFGAVFGY LSLWSVFWLF KLVTGKEGMG YGDFKLLAML GAWGGWQILP LTILLSSLVG AILGVIMLRL RNAESGTPIP FGPYLAIAGW IALLWGDQIT RTYLQFAGFK //