ID A0A1M6LH38_9CLOT Unreviewed; 253 AA.
AC A0A1M6LH38;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Leader peptidase (Prepilin peptidase) / N-methyltransferase {ECO:0000313|EMBL:SHJ70458.1};
GN ORFNames=SAMN02745248_00755 {ECO:0000313|EMBL:SHJ70458.1};
OS Hathewaya proteolytica DSM 3090.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hathewaya.
OX NCBI_TaxID=1121331 {ECO:0000313|EMBL:SHJ70458.1, ECO:0000313|Proteomes:UP000183952};
RN [1] {ECO:0000313|EMBL:SHJ70458.1, ECO:0000313|Proteomes:UP000183952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3090 {ECO:0000313|EMBL:SHJ70458.1,
RC ECO:0000313|Proteomes:UP000183952};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRAD01000005; SHJ70458.1; -; Genomic_DNA.
DR RefSeq; WP_072902500.1; NZ_FRAD01000005.1.
DR AlphaFoldDB; A0A1M6LH38; -.
DR STRING; 1121331.SAMN02745248_00755; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000183952; 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:SHJ70458.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183952};
KW Transferase {ECO:0000313|EMBL:SHJ70458.1};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..94
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 104..209
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 253 AA; 28136 MW; A4AC009283826513 CRC64;
MDYLIYAIIF FMGASVGSFL NVCASRIPAE ESIVKPPSHC NDCGYVLAWY DLIPLFSWLF
LRGKCRKCGA KLSSRYFFVE LFTGLMFLLL FMEFGVSLKF AVYLIFTCFL IVIGLIDFDT
QDIYDIHIIA PAVVQLVFIA YMFLKGENVM TYFYGALAGG GFISLIVILT HGMGWGDAEL
CALCGLVLGF KYTLLTIFIA IVLGGIVGVI VLLTRKKGRK DAIAFGPFIA MGAMAAMLWG
QQLIDCYVRL IVR
//
