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Database: UniProt
Entry: A0A1G1V450_9BACT
LinkDB: A0A1G1V450_9BACT
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ID   A0A1G1V450_9BACT        Unreviewed;       154 AA.
AC   A0A1G1V450;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Prepilin type IV endopeptidase peptidase domain-containing protein {ECO:0000259|Pfam:PF01478};
GN   ORFNames=A3F61_02120 {ECO:0000313|EMBL:OGY10136.1};
OS   Candidatus Blackburnbacteria bacterium RIFCSPHIGHO2_12_FULL_41_13b.
OC   Bacteria; Candidatus Blackburnbacteria.
OX   NCBI_TaxID=1797517 {ECO:0000313|EMBL:OGY10136.1, ECO:0000313|Proteomes:UP000178272};
RN   [1] {ECO:0000313|EMBL:OGY10136.1, ECO:0000313|Proteomes:UP000178272}
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   -!- 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:OGY10136.1}.
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DR   EMBL; MHCA01000060; OGY10136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1V450; -.
DR   STRING; 1797517.A3F61_02120; -.
DR   Proteomes; UP000178272; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.1220; -; 1.
DR   InterPro; IPR014032; Peptidase_A24A_bac.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
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; PF01478; Peptidase_A24; 1.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        29..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        122..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..112
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   154 AA;  17538 MW;  E2D51D1AB5633F17 CRC64;
     MALPYLLVIV MVLIALAVVD IERQILPDSL IYFLGFIFAV YFILFVHNLL FSHLLWGYLS
     FLFFLTIYLV TKRRGMGFGD VKLSFVLGSF LGFPQFVIWL FGAFTLGAVV GLILLAVRRA
     KLGLPIPFGP FLLVSFWLTV FYGEKIAGWY LKLL
//
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