ID Q5E2R3_VIBF1 Unreviewed; 295 AA. AC Q5E2R3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-APR-2010, entry version 37. DE SubName: Full=PilD; DE SubName: Full=Type 4 prepilin peptidase PilD; DE EC=3.4.-.-; GN Name=pilD; OrderedLocusNames=VF_2188; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES114; 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). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ES114; RA Browne-Silva J.K., Nishiguchi M.K.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates CC the N-terminal (generally Phe) residue (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By CC similarity). CC -!- SIMILARITY: Belongs to the peptidase A24 family. 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; YP_205571.1; -. DR STRING; Q5E2R3; -. DR MEROPS; A24.001; -. DR GeneID; 3279527; -. DR GenomeReviews; CP000020_GR; VF_2188. DR KEGG; vfi:VF_2188; -. DR NMPDR; fig|312309.3.peg.2188; -. DR eggNOG; COG1989; -. DR HOGENOM; HBG710101; -. DR OMA; DHQLLPD; -. DR PhylomeDB; Q5E2R3; -. DR ProtClustDB; CLSK874797; -. DR BioCyc; VFIS312309:VF2188-MONOMER; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR InterPro; IPR010627; Pept_A24A_N. DR InterPro; IPR014032; Peptidase_A24A_bac. DR InterPro; IPR000045; Peptidase_A24A_prepilin_IV. 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; Hydrolase; Protease; Transmembrane. 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 //