ID O68839_VIBCL Unreviewed; 291 AA. AC O68839; Q7DCT3; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 145. 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:AAD21032.1}; GN ORFNames=BC353_07390 {ECO:0000313|EMBL:RGP91607.1}, D6U24_03850 GN {ECO:0000313|EMBL:MVD22484.1}, FLM02_13485 GN {ECO:0000313|EMBL:TQP12028.1}; OS Vibrio cholerae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=666 {ECO:0000313|EMBL:AAC63504.1}; RN [1] {ECO:0000313|EMBL:AAC63504.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C6706str2 {ECO:0000313|EMBL:AAC63504.1}; RX PubMed=9781884; DOI=10.1046/j.1365-2958.1998.01031.x; RA Marsh J.W., Taylor R.K.; RT "Identification of the Vibrio cholerae type 4 prepilin peptidase required RT for cholera toxin secretion and pilus formation."; RL Mol. Microbiol. 29:1481-1492(1998). RN [2] {ECO:0000313|EMBL:AAD21032.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=10024587; RA Fullner K.J., Mekalanos J.J.; RT "Genetic characterization of a new type IV-A pilus gene cluster found in RT both classical and El Tor biotypes of Vibrio cholerae."; RL Infect. Immun. 67:1393-1404(1999). RN [3] {ECO:0000313|EMBL:RGP91607.1, ECO:0000313|Proteomes:UP000266701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VN-2825 {ECO:0000313|EMBL:RGP91607.1, RC ECO:0000313|Proteomes:UP000266701}; RX PubMed=28930017; DOI=10.3201/eid2310.161625; RA Hammerl J.A., Jackel C., Bortolaia V., Schwartz K., Bier N., RA Hendriksen R.S., Guerra B., Strauch E.; RT "Carbapenemase VCC-1-Producing Vibrio cholerae in Coastal Waters of RT Germany."; RL Emerg. Infect. Dis. 23:1735-1737(2017). RN [4] {ECO:0000313|EMBL:MVD22484.1, ECO:0000313|Proteomes:UP000471242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=00-1_S85 {ECO:0000313|EMBL:MVD22484.1, RC ECO:0000313|Proteomes:UP000471242}; RA Wang H., Zen W., Yu H., Zhang W., Pan J., Yang C., Cui Y.; RT "Genomic epidemiology reveals two lineages of Vibrio cholerae that can RT cause global cholera epidemics despite absence of cholera toxin gene."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:TQP12028.1, ECO:0000313|Proteomes:UP000319979} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A12JL36W90 {ECO:0000313|EMBL:TQP12028.1, RC ECO:0000313|Proteomes:UP000319979}; RA Lepuschitz S., Baron S., Larvor E., Granier S., Pretzer C., Mach R.L., RA Farnleitner A.H., Ruppitsch W., Pleininger S., Indra A., Kirschner A.K.T.; RT "Phenotypic and genotypic antimicrobial resistance traits of Vibrio RT cholerae non-O1/non-O139 isolated from a large Austrian lake frequently RT associated with cases of infection."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. 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; AF055371; AAC63504.1; -; Genomic_DNA. DR EMBL; AF109904; AAD21032.1; -; Genomic_DNA. DR EMBL; QZRB01000004; MVD22484.1; -; Genomic_DNA. DR EMBL; MCBA01000002; RGP91607.1; -; Genomic_DNA. DR EMBL; VIOS01000051; TQP12028.1; -; Genomic_DNA. DR PIR; B82078; B82078. DR RefSeq; WP_000418747.1; NZ_WYCS01000092.1. DR MEROPS; A24.001; -. DR DNASU; 2612968; -. DR GeneID; 69718967; -. DR KEGG; vcq:EN18_15165; -. DR PATRIC; fig|666.1968.peg.2720; -. DR OMA; VFWLFKL; -. DR PHI-base; PHI:702; -. DR Proteomes; UP000266701; Unassembled WGS sequence. DR Proteomes; UP000319979; Unassembled WGS sequence. DR Proteomes; UP000471242; Unassembled WGS sequence. 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; IPR014032; Peptidase_A24A_bac. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR InterPro; IPR010627; Prepilin_pept_A24_N. 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; A24_N_bact; 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}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000256|RuleBase:RU003794, KW ECO:0000313|EMBL:RGP91607.1}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU003794}; KW Protease {ECO:0000256|RuleBase:RU003794}; KW Transferase {ECO:0000256|RuleBase:RU003794, ECO:0000313|EMBL:RGP91607.1}; 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..30 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 112..145 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 157..174 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 181..199 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 219..245 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 257..275 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 17..124 FT /note="Prepilin peptidase A24 N-terminal" FT /evidence="ECO:0000259|Pfam:PF06750" FT DOMAIN 134..244 FT /note="Prepilin type IV endopeptidase peptidase" FT /evidence="ECO:0000259|Pfam:PF01478" SQ SEQUENCE 291 AA; 32434 MW; 9A1ECD8D730A6EEF CRC64; MELFYFYPWL FPVLATLFGL IVGSFLNVVI YRLPKIMERE WRAECAASFP EYGITPPEGK LTLSLPRSTC PHCQTPIRVI DNIPLLSWLA LRGQCSHCKA PISARYPLIE LLTALMSLVI ATHFPFGVFA VALLFFSYVL IAATFIDFDT LLLPDQLTLP LLWGGIALAL LGFSPVSLSD AVIGAMAGYL SLWSIYWLFK LLTGKEGMGY GDFKLLAALG AWLGWQQLPV IVLLSSVVGV IFGLIQLRQQ KKGIDMAFPF GPYLAIAGWF ALLWGDKVID WYFTTWVGQP L //