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Database: UniProt
Entry: B1V3E4_CLOPF
LinkDB: B1V3E4_CLOPF
Original site: B1V3E4_CLOPF 
ID   B1V3E4_CLOPF            Unreviewed;       247 AA.
AC   B1V3E4;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Type IV leader peptidase family protein {ECO:0000313|EMBL:EDT71698.1};
GN   ORFNames=CJD_2897 {ECO:0000313|EMBL:EDT71698.1};
OS   Clostridium perfringens D str. JGS1721.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT71698.1, ECO:0000313|Proteomes:UP000003188};
RN   [1] {ECO:0000313|EMBL:EDT71698.1, ECO:0000313|Proteomes:UP000003188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D str. JGS1721 {ECO:0000313|Proteomes:UP000003188};
RA   Paulsen I., Sebastian Y.;
RL   Submitted (MAR-2008) 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}.
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:EDT71698.1}.
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DR   EMBL; ABOO01000018; EDT71698.1; -; Genomic_DNA.
DR   RefSeq; WP_003475074.1; NZ_ABOO01000018.1.
DR   AlphaFoldDB; B1V3E4; -.
DR   Proteomes; UP000003188; 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        189..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        222..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..87
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
FT   DOMAIN          100..206
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   247 AA;  27546 MW;  4689D962ECE294D1 CRC64;
     MSIIFFLFGL IIGSFLNVCI FRIPAGESIA FPPSHCGTCK KQLKPIDLVP VFSYLFLGGK
     CRYCKNKISI RYPLIELLTG FLYFCVYKYY GISFLTVKYI VLITFLIVIS FIDYDTQDVY
     AVTTYPAVIL GIIFALIEKF YFGENLLNYF MGLVISALVI FLISKLTGAM GSGDIEIHAI
     AGIFLGWKLA IINIFLSFII GGIIAVLAIL FKQKKKGDYI AFGPAIGIST IILIFFGNII
     IPIYFGV
//
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