ID Q5E2R3_VIBF1 Unreviewed; 295 AA. AC Q5E2R3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. 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 Name=pilD {ECO:0000313|EMBL:AAW86683.1}; GN OrderedLocusNames=VF_2188 {ECO:0000313|EMBL:AAW86683.1}; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86683.1, ECO:0000313|Proteomes:UP000000537}; RN [1] {ECO:0000313|EMBL:AAW86683.1, ECO:0000313|Proteomes:UP000000537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537}, and RC ES114 {ECO:0000313|EMBL:AAW86683.1}; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). RN [2] {ECO:0000313|EMBL:ABC11895.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES114 {ECO:0000313|EMBL:ABC11895.1}; RA Browne-Silva J.K., Nishiguchi M.K.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AAW86683.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES114 {ECO:0000313|EMBL:AAW86683.1}; RX PubMed=18366731; DOI=10.1186/1471-2164-9-138; RA Mandel M.J., Stabb E.V., Ruby E.G.; RT "Comparative genomics-based investigation of resequencing targets in RT Vibrio fischeri: focus on point miscalls and artefactual expansions."; RL BMC Genomics 9:138-138(2008). RN [4] {ECO:0000313|EMBL:ABC11895.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES114 {ECO:0000313|EMBL:ABC11895.1}; RX PubMed=18523167; DOI=10.1099/ijs.0.65370-0; RA Browne-Silva J., Nishiguchi M.K.; RT "Gene sequences of the pil operon reveal relationships between RT symbiotic strains of Vibrio fischeri."; RL Int. J. Syst. Evol. Microbiol. 58:1292-1299(2008). 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: Cell membrane CC {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003794}. CC -!- SIMILARITY: Belongs to the peptidase A24 family. CC {ECO:0000256|RuleBase:RU003793}. 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; CP000020; AAW86683.1; -; Genomic_DNA. DR EMBL; DQ093345; ABC11895.1; -; Genomic_DNA. DR RefSeq; WP_011262625.1; NC_006840.2. DR RefSeq; YP_205571.1; NC_006840.2. DR STRING; 312309.VF_2188; -. DR EnsemblBacteria; AAW86683; AAW86683; VF_2188. DR GeneID; 3279527; -. DR KEGG; vfi:VF_2188; -. DR PATRIC; 20115122; VBIVibFis127983_2228. DR eggNOG; ENOG4105EHH; Bacteria. DR eggNOG; COG1989; LUCA. DR HOGENOM; HOG000248584; -. DR KO; K02654; -. DR OMA; VFWLFKL; -. DR OrthoDB; EOG6F55M8; -. DR BioCyc; AFIS312309:GIWP-2313-MONOMER; -. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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 Complete proteome {ECO:0000313|Proteomes:UP000000537}; KW Hydrolase {ECO:0000256|RuleBase:RU003794, KW ECO:0000313|EMBL:AAW86683.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000256|RuleBase:RU003794}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU003794}; KW Protease {ECO:0000256|RuleBase:RU003794}; KW Reference proteome {ECO:0000313|Proteomes:UP000000537}; KW Transferase {ECO:0000256|RuleBase:RU003794}; KW Transmembrane {ECO:0000256|RuleBase:RU003794, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 235 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 287 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 17 126 DiS_P_DiS. {ECO:0000259|Pfam:PF06750}. FT DOMAIN 139 248 Peptidase_A24. {ECO:0000259|Pfam: FT PF01478}. SQ SEQUENCE 295 AA; 33133 MW; 7B2FEC9CF5F68DEB CRC64; MAVFDYYPWL FPLFATLFGL LVGSFLNVVI YRLPIMMEKE WKKDCIDCFP DLAPKKTSEE KEETFNLSVP RSRCPKCQTQ IKFYDNIPVI SWLLLKGKCR QCSNPISFRY PAIELLSGAM CFAVSYLLPF SYFAVAAVLF TLVLIALTFI DIDTMLLPDQ ITLPLLWSGL YLALVGWSSV SLVDSVVGAM AGYLILWSIY WGFKLLTGKE GMGYGDFKLL AALGAWLGWQ QLPLIILLSS VVGAIIGVIM LTAQKKGFDK AIPFGPYLAI AGWVCLLWGQ NISQWYFNHI LGLPL //