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Database: UniProt
Entry: A0A1F8PFI8_9CHLR
LinkDB: A0A1F8PFI8_9CHLR
Original site: A0A1F8PFI8_9CHLR 
ID   A0A1F8PFI8_9CHLR        Unreviewed;       188 AA.
AC   A0A1F8PFI8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=Prepilin type IV endopeptidase peptidase domain-containing protein {ECO:0000259|Pfam:PF01478};
GN   ORFNames=A2Y54_07435 {ECO:0000313|EMBL:OGO21897.1};
OS   Chloroflexi bacterium RBG_16_51_16.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797644 {ECO:0000313|EMBL:OGO21897.1, ECO:0000313|Proteomes:UP000178729};
RN   [1] {ECO:0000313|EMBL:OGO21897.1, ECO:0000313|Proteomes:UP000178729}
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}.
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:OGO21897.1}.
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DR   EMBL; MGNL01000146; OGO21897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8PFI8; -.
DR   Proteomes; UP000178729; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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.
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..141
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   188 AA;  20801 MW;  DF764C8AD5B0E2F5 CRC64;
     MSVYIWLNPP HNLGYLLGMA LITYFAVVFV IDMENRLILH PTSLVGAGLA LIAGWLVHGI
     ARSVFGGIAG FLFMLILYYF GVLFARYRTR RMQASGFTPD DEEVLGAGDV ILAGILGLAL
     GWPLIWFGIL LGILLGGVYG IFLVLAMVLT RNIKGRALQI FMPYGPFFIL SAVFIIFLPH
     FIRYMLPG
//
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