ID Q5E2R3_ALIF1 Unreviewed; 295 AA. AC Q5E2R3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 28-JUN-2023, entry version 100. DE RecName: Full=Prepilin leader peptidase/N-methyltransferase {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 Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC 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 with RT 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 Vibrio RT 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 symbiotic RT strains of Vibrio fischeri."; RL Int. J. Syst. Evol. Microbiol. 58:1292-1299(2008). CC -!- FUNCTION: Plays an essential role in type IV pili and type II CC pseudopili formation by proteolytically removing the leader sequence CC from substrate proteins and subsequently monomethylating the alpha- CC amino group of the newly exposed N-terminal phenylalanine. CC {ECO:0000256|RuleBase:RU003794}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, CC basic peptide of 5-8 residues from type IV prepilin, and then N- CC methylates the new N-terminal amino group, the methyl donor being S- CC adenosyl-L-methionine.; EC=3.4.23.43; CC Evidence={ECO:0000256|RuleBase:RU003794}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004429}. Cell membrane CC {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003794}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the peptidase A24 family. CC {ECO:0000256|ARBA:ARBA00005801, 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 MEROPS; A24.001; -. DR EnsemblBacteria; AAW86683; AAW86683; VF_2188. DR KEGG; vfi:VF_2188; -. DR PATRIC; fig|312309.11.peg.2228; -. DR eggNOG; COG1989; Bacteria. DR HOGENOM; CLU_057101_0_0_6; -. DR OMA; GAWGGWQ; -. DR OrthoDB; 9789291at2; -. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.1220; -; 1. DR InterPro; IPR010627; Pept_A24A_N. DR InterPro; IPR014032; Peptidase_A24A_bac. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR PANTHER; PTHR30487:SF0; PREPILIN LEADER PEPTIDASE/N-METHYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR30487; TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME; 1. DR Pfam; PF06750; DiS_P_DiS; 1. DR Pfam; PF01478; Peptidase_A24; 1. DR PRINTS; PR00864; PREPILNPTASE. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Hydrolase {ECO:0000256|RuleBase:RU003794, ECO:0000313|EMBL:AAW86683.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003794}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 6..33 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 132..150 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 162..180 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 186..203 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 235..253 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 265..287 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 17..126 FT /note="Peptidase A24A N-terminal" FT /evidence="ECO:0000259|Pfam:PF06750" FT DOMAIN 139..248 FT /note="Prepilin type IV endopeptidase peptidase" FT /evidence="ECO:0000259|Pfam: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 //