ID E6WQQ9_PSEUU Unreviewed; 287 AA.
AC E6WQQ9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=Psesu_0652 {ECO:0000313|EMBL:ADV26508.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV26508.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV26508.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) 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; CP002446; ADV26508.1; -; Genomic_DNA.
DR RefSeq; WP_013534338.1; NC_014924.1.
DR AlphaFoldDB; E6WQQ9; -.
DR STRING; 743721.Psesu_0652; -.
DR MEROPS; A24.001; -.
DR KEGG; psu:Psesu_0652; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_0_6; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000008632; Chromosome.
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:ADV26508.1};
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:UP000008632};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..123
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 134..241
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 287 AA; 31841 MW; C02E82017B9F704B CRC64;
MAFLDQQPLL GYPLIAGVGL AVGSFLNVVI LRLPRRLEWE WKRDAREVLG EPEIYDPPPP
GVVVEPSHDP VTGDRLKWWE NIPVLSWLML RGRSRYSGQR ISIQYPLVEL LTGLLTVACA
WRFGFGWQGF GAMLLTWYLV ALSGIDLRTR LLPDQLTLPL MWLGLIASLD NLYMPAKPAL
LGAVAGYVSL WSVWWLFKQL TGKEGMGHGD FKLLAALGAW CGLKGILPII LLSSVVGAVI
GSVWLAYKGR DRATPIPFGP YLAIAGWIFF FWGDSLLGAY RSYAGLG
//
