ID   A0A0J1D9L9_9BURK        Unreviewed;       180 AA.
AC   A0A0J1D9L9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Prepilin type IV endopeptidase peptidase domain-containing protein {ECO:0000259|Pfam:PF01478};
GN   ORFNames=AB595_16235 {ECO:0000313|EMBL:KLU35803.1};
OS   Massilia sp. WF1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU35803.1, ECO:0000313|Proteomes:UP000036336};
RN   [1] {ECO:0000313|Proteomes:UP000036336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA   Lou J., Gu H., Wang H., Xu J.;
RT   "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT   strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT   contaminated soil.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KLU35803.1}.
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DR   EMBL; LELH02000020; KLU35803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1D9L9; -.
DR   PATRIC; fig|1406431.3.peg.2343; -.
DR   Proteomes; UP000036336; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000036336};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        32..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..116
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   180 AA;  18436 MW;  AAEE4C34ACFECF26 CRC64;
     MTNFVEPGAG QLVMLVVLLL VATVLDVRQG RIPNWLVGSG MLGALVFHGI SPQGEGIAFA
     LAGLALGMAA LLPLYMLRVM GAGDVKLMGM TGAFLGMSGV LGAILASLAA GGILAIAMAA
     GKRMLPQLLA NLRGIVVQYH IGHITRDLSG IVRPAASVGS MPYAAAITAG TLAQLLFLRY
//