ID K0XMU9_PSEAI Unreviewed; 290 AA. AC K0XMU9; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 04-MAR-2015, entry version 12. DE RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme {ECO:0000256|RuleBase:RU003794}; DE EC=2.1.1.- {ECO:0000256|RuleBase:RU003794}; DE EC=3.4.23.43 {ECO:0000256|RuleBase:RU003794}; GN ORFNames=A161_22513 {ECO:0000313|EMBL:EJZ72418.1}; OS Pseudomonas aeruginosa PAO579. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1191475 {ECO:0000313|EMBL:EJZ72418.1}; RN [1] {ECO:0000313|EMBL:EJZ72418.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PAO579 {ECO:0000313|EMBL:EJZ72418.1}; 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. CC {ECO:0000256|RuleBase:RU003794}. 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 {ECO:0000256|RuleBase:RU003794}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003794}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003794}. CC -!- SIMILARITY: Belongs to the peptidase A24 family. CC {ECO:0000256|RuleBase:RU003793}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJZ72418.1}. 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 EnsemblBacteria; EJZ72418; EJZ72418; A161_22513. DR GO; GO:0016021; C:integral component of 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 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 {ECO:0000256|RuleBase:RU003794}; KW Membrane {ECO:0000256|RuleBase:RU003794}; KW Methyltransferase {ECO:0000256|RuleBase:RU003794}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU003794}; KW Protease {ECO:0000256|RuleBase:RU003794}; KW Transferase {ECO:0000256|RuleBase:RU003794}; KW Transmembrane {ECO:0000256|RuleBase:RU003794}. 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 //