ID A0A1G1W3H4_9BACT Unreviewed; 269 AA.
AC A0A1G1W3H4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=A2113_03095 {ECO:0000313|EMBL:OGY22238.1};
OS Candidatus Woykebacteria bacterium GWA1_44_8.
OC Bacteria; Candidatus Woykebacteria.
OX NCBI_TaxID=1802591 {ECO:0000313|EMBL:OGY22238.1, ECO:0000313|Proteomes:UP000176299};
RN [1] {ECO:0000313|EMBL:OGY22238.1, ECO:0000313|Proteomes:UP000176299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGY22238.1}.
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DR EMBL; MHCN01000007; OGY22238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1W3H4; -.
DR STRING; 1802591.A2113_03095; -.
DR Proteomes; UP000176299; 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 Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW Protease {ECO:0000256|RuleBase:RU003794};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..93
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 113..224
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 269 AA; 29125 MW; 902A69D119FF6F2A CRC64;
MIQILTILFF IIGTAVGSFL NVVAYRSVHG GSVFFGSSIC PKCKHKLGPS DLVPIVSFLL
LNGRCRYCHK KISLQYPLVE LATGLLFAFT FLHGYYLTNS INSINLIHLI YLLFIVSTLT
VLFTTDLRSG LLPNSIVLPA IAAVAVFKII LLAFSDSDSV YGLSADLVAS FLVASAFFAI
VYLSRERALG GGDIKFVFLI ALAVGWPALL VALWLAFLTG GLVAAMLILL GKKRFGQTVP
LGPFLAFGGL IALLLGQQII DLYLKGLYR
//
