ID   A0A0G1D0R3_9BACT        Unreviewed;       250 AA.
AC   A0A0G1D0R3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Type 4 prepilin-like protein leader peptide-processing enzyme {ECO:0000313|EMBL:KKS91525.1};
GN   ORFNames=UV65_C0004G0015 {ECO:0000313|EMBL:KKS91525.1};
OS   Parcubacteria group bacterium GW2011_GWF2_43_11.
OC   Bacteria.
OX   NCBI_TaxID=1618967 {ECO:0000313|EMBL:KKS91525.1, ECO:0000313|Proteomes:UP000034303};
RN   [1] {ECO:0000313|EMBL:KKS91525.1, ECO:0000313|Proteomes:UP000034303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801}.
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:KKS91525.1}.
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DR   EMBL; LCFH01000004; KKS91525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1D0R3; -.
DR   Proteomes; UP000034303; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.1220; -; 1.
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.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        223..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..93
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          102..207
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   250 AA;  28332 MW;  9AD24CE4518E46BB CRC64;
     MATPFLFFIV LLFGLTAGSF LNCVVYRLEN NQSFLTGRSF CPKCKHVLAW YDLMPVLSFL
     LLGGKCRHCQ KKISFQYPLV EIAVALLFLA IFYYRLPVFS YFLSLFLIVI FIYDLKHYLI
     LDKVIYPAIG LTLIYDLLRF DLFTNWNLLI SAIGASGFFL LIVLASRGKW MGVGDIKLAF
     LMGLILGWPN ILVALFFAFL SGATIGVGLV LARRKSFKSE VPFGPFLVAG TIVAMFYGQA
     LINWYLNLYV
//