ID A0A1I7HQK5_9FIRM Unreviewed; 262 AA.
AC A0A1I7HQK5;
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:SFU63025.1};
GN ORFNames=SAMN05216508_12213 {ECO:0000313|EMBL:SFU63025.1};
OS Eubacterium pyruvativorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=155865 {ECO:0000313|EMBL:SFU63025.1, ECO:0000313|Proteomes:UP000198817};
RN [1] {ECO:0000313|EMBL:SFU63025.1, ECO:0000313|Proteomes:UP000198817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHGC13 {ECO:0000313|EMBL:SFU63025.1,
RC ECO:0000313|Proteomes:UP000198817};
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; FPBT01000022; SFU63025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7HQK5; -.
DR STRING; 155865.SAMN05216515_12512; -.
DR Proteomes; UP000198817; 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:SFU63025.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198817};
KW Transferase {ECO:0000313|EMBL:SFU63025.1};
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 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..101
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 111..225
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 262 AA; 28258 MW; 7488A5C5CCA3876D CRC64;
MLQISGIITA YCTVLAAVLG AVFGSFLNCM AWRIAHHESV ITGRSHCPVC GHVLGPGDLV
PVFSWIFLKG KCRYCGAPVS VRYLLTEVFS AAGFVLILFR FDVSWTLLRY LVLFCILLTL
SLVDLEIFEI PDRFIAAGIL WWAVTLLPAA ESGTSFGRQL LTGLTGGALV GGGMLLLTLL
FDRATGKESM GGGDIKLFFM TGLYLGPAGA LLGLILSCVL GLVFAAASRR RKIPFGPAIS
LSAMLVLLWG RPVIEWYMGF LS
//
