ID   A0A1I0ZGV7_9BACI        Unreviewed;       253 AA.
AC   A0A1I0ZGV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Leader peptidase (Prepilin peptidase) / N-methyltransferase {ECO:0000313|EMBL:SFB25009.1};
GN   ORFNames=SAMN04488072_11198 {ECO:0000313|EMBL:SFB25009.1};
OS   Lentibacillus halodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=237679 {ECO:0000313|EMBL:SFB25009.1, ECO:0000313|Proteomes:UP000198642};
RN   [1] {ECO:0000313|EMBL:SFB25009.1, ECO:0000313|Proteomes:UP000198642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3702 {ECO:0000313|EMBL:SFB25009.1,
RC   ECO:0000313|Proteomes:UP000198642};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FOJW01000011; SFB25009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0ZGV7; -.
DR   STRING; 237679.SAMN04488072_11198; -.
DR   OrthoDB; 9789291at2; -.
DR   Proteomes; UP000198642; 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   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   Methyltransferase {ECO:0000313|EMBL:SFB25009.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198642};
KW   Transferase {ECO:0000313|EMBL:SFB25009.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        122..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..93
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          104..208
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   253 AA;  28304 MW;  22CF561EE54A7E8F CRC64;
     MDNLLILLFF LLGLIFGSFF NVIGLRIPQK KSFTNDRSVC PQCQHPLSWP ELIPVLSYMM
     QRGKCRHCNG SISLLYPVIE LTTGVLFVFC YIQSGLDFEL ITALILMSLL VIILVSDIRY
     MLIPNSILLF FFPLLVLARF IRPLDTWWSS IAGAFAGVLI IAIVILVSRG GMGAGDMKLF
     GLLGIVLGFE KTLLALFLSC MIGAVIGLVL LLLKVIDRQQ PVPFGPYIVI ASIITYFHGD
     ILLGWYFHDW LQG
//