ID D0YWB0_PHODD Unreviewed; 292 AA.
AC D0YWB0;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=VDA_001188 {ECO:0000313|EMBL:EEZ40166.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ40166.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ40166.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ40166.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) 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}.
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DR EMBL; ADBS01000001; EEZ40166.1; -; Genomic_DNA.
DR RefSeq; WP_005297598.1; NZ_ADBS01000001.1.
DR AlphaFoldDB; D0YWB0; -.
DR MEROPS; A24.001; -.
DR eggNOG; COG1989; Bacteria.
DR Proteomes; UP000003579; 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, ECO:0000313|EMBL:EEZ40166.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW ECO:0000313|EMBL:EEZ40166.1};
KW Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW Protease {ECO:0000256|RuleBase:RU003794};
KW Reference proteome {ECO:0000313|Proteomes:UP000003579};
KW Transferase {ECO:0000256|RuleBase:RU003794, ECO:0000313|EMBL:EEZ40166.1};
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 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..126
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 137..247
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 292 AA; 32501 MW; 54E671135608F146 CRC64;
MAIFSYYPWL FPVFATIFGL LVGSFLNVVI YRLPIMMERQ WRNECIEAFP DLIKADAKLN
TDTFNLSVPR SRCPHCGHLI SAVENIPVIS WLALKGKCKS CHAPISRRYP MIELLTAALC
GTVAILFPPT WWAVAVIFFT FALIALTFID IDKMLLPDQI TLPLLWAGIF LALLGISPVS
LQDSVIGAIA GYLCLWSVFW IFKLLTKKDG MGYGDFKLLA ALGAWLGWQM LPVVVLLSSL
AGAICGIILL KVQKSDHQTP FSFGPYLAIA GWISLLWGHS IITWYVSNIL GM
//
