ID A0A1L4C0H1_9LACT Unreviewed; 250 AA.
AC A0A1L4C0H1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Prepilin peptidase {ECO:0000313|EMBL:API89601.1};
GN ORFNames=BKP56_10180 {ECO:0000313|EMBL:API89601.1};
OS Marinilactibacillus sp. 15R.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Marinilactibacillus.
OX NCBI_TaxID=1911586 {ECO:0000313|EMBL:API89601.1, ECO:0000313|Proteomes:UP000184433};
RN [1] {ECO:0000313|EMBL:API89601.1, ECO:0000313|Proteomes:UP000184433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15R {ECO:0000313|EMBL:API89601.1,
RC ECO:0000313|Proteomes:UP000184433};
RA Wei Y., Cao J., Fang J.;
RT "Genome sequence of Marinilactibacillus sp. 15R.";
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; CP017761; API89601.1; -; Genomic_DNA.
DR RefSeq; WP_072694990.1; NZ_CP017761.1.
DR AlphaFoldDB; A0A1L4C0H1; -.
DR STRING; 1911586.BKP56_10180; -.
DR KEGG; marr:BKP56_10180; -.
DR Proteomes; UP000184433; Chromosome.
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:UP000184433};
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..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..204
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..206
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 250 AA; 28003 MW; 3A509DA021707AC9 CRC64;
MEWFIGIVFF IYGLIFGSFY NVVGLRVPVN TFFAQKNSYC YTCKRKLSWS ELIPVVSYIF
QKGKCKGCGD SISIIYPVVE LTTGLLFVAT YLFFGVSFQT IFGLLLVSMI VIVTVSDIAY
QKIPNKILLF FLPILLILKF FLLDTDWISS IFGAASAFLL VGIIIYVTKG GMGIGDLKYF
TLFGLLFGWQ LFLLLFLLST LYGAVINGIL LSLGKVTRKT KVPFGPYIGA SAITVLYLGR
SIIEWYLSLL
//
