ID   A0A1G8LS23_9BACI        Unreviewed;       249 AA.
AC   A0A1G8LS23;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Type 4 prepilin peptidase 1 Aspartic peptidase. MEROPS family A24A {ECO:0000313|EMBL:SDI58423.1};
GN   ORFNames=SAMN04488123_103239 {ECO:0000313|EMBL:SDI58423.1};
OS   Natribacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Natribacillus.
OX   NCBI_TaxID=549003 {ECO:0000313|EMBL:SDI58423.1, ECO:0000313|Proteomes:UP000198853};
RN   [1] {ECO:0000313|EMBL:SDI58423.1, ECO:0000313|Proteomes:UP000198853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21771 {ECO:0000313|EMBL:SDI58423.1,
RC   ECO:0000313|Proteomes:UP000198853};
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; FNEN01000003; SDI58423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8LS23; -.
DR   OrthoDB; 9789291at2; -.
DR   Proteomes; UP000198853; 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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198853};
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..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..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..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..92
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          104..205
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   249 AA;  27667 MW;  534A40212EFCFC11 CRC64;
     MLFDVIVFLL LGLVLGSFFQ VVGMRVPSGE PFAWSRSVCP HCRTTLQARD LWPVLSYLFT
     MGKCRYCGTR ISGQYVLVEL STAFLFVLAY FRYQFTLDTM LALLVLSLVM IVTITDLRYM
     RIPNAILLFF ASCLLLIRIF VAPYDPWWDP FLAALLSFSV LYGVMIMSGG GLGGGDVKLF
     AVLGLAFGLW DLLLVFFLST LFGTLSSLAA FASGHLKRGQ AFPFAPSIAL AGIVVLFIGD
     WLWGLYPVM
//