ID A0A1G4VN62_9FIRM Unreviewed; 254 AA.
AC A0A1G4VN62;
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:SCX08788.1};
GN ORFNames=SAMN02910339_01286 {ECO:0000313|EMBL:SCX08788.1};
OS Lachnospiraceae bacterium YSD2013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520828 {ECO:0000313|EMBL:SCX08788.1, ECO:0000313|Proteomes:UP000199278};
RN [1] {ECO:0000313|EMBL:SCX08788.1, ECO:0000313|Proteomes:UP000199278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSD2013 {ECO:0000313|EMBL:SCX08788.1,
RC ECO:0000313|Proteomes:UP000199278};
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; FMTX01000011; SCX08788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4VN62; -.
DR STRING; 1520828.SAMN02910339_01286; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000199278; 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:SCX08788.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199278};
KW Transferase {ECO:0000313|EMBL:SCX08788.1};
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 89..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..96
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 108..210
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 254 AA; 28217 MW; F69E7304EEB4A967 CRC64;
MPAELLIPIY IFVFLFGIVI GSFLNVCMIR IPRGESIVTE GSHCMKCGYR LRWYDLIPLF
SWLFLRGKCR KCGEKISPQY PVVEFINGAV YVFVFVLKGI TIESLLLCLL FSALFTLSVI
DFKTYEIPVG FNIFIAVLGL VRLFTDLSNW KDYLIGAVSI SLFLLILLLV SKGRAIGGGD
VKLMAAAGLF LGWKCAILAF MVGCILGACI HLIRMKVSKE GSVLAMGPYL SAGIFIAALW
GVNIITWYLG FYAF
//
