GenomeNet

Database: UniProt
Entry: A0A1F5G1Z7_9BACT
LinkDB: A0A1F5G1Z7_9BACT
Original site: A0A1F5G1Z7_9BACT 
ID   A0A1F5G1Z7_9BACT        Unreviewed;       256 AA.
AC   A0A1F5G1Z7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Prepilin peptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2164_02990 {ECO:0000313|EMBL:OGD85906.1};
OS   Candidatus Curtissbacteria bacterium RBG_13_35_7.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1797705 {ECO:0000313|EMBL:OGD85906.1, ECO:0000313|Proteomes:UP000176317};
RN   [1] {ECO:0000313|EMBL:OGD85906.1, ECO:0000313|Proteomes:UP000176317}
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   -!- 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:OGD85906.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MFAT01000052; OGD85906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5G1Z7; -.
DR   Proteomes; UP000176317; 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};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          10..90
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          108..212
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   256 AA;  28979 MW;  74B02A3B5592101A CRC64;
     MFFYLFVSFI LGSAVGSFLN VVIDRTTRGE SIRGRSYCDH CRVTLSTLDL IPIISFIVFR
     AKCRYCKKPL SWQYPLIESL TAILFTLAFY ILAKNSNLAI IPLLYYFLII SVSIIVAVVD
     LKYYLIPTTF VYIASIIALF YNYLFLSSTL FVEHVIAGFV IAFLFLLIVL VTRGRGMGQG
     DIVLVFLMGM VLGYKGTFVA IFLAFLTGAI VSVALIISRK KHFGQTVPFA PFLILGFLTS
     LFWSEQLLNI YLQMLY
//
DBGET integrated database retrieval system