ID A0A1C4VLS6_9ACTN Unreviewed; 278 AA.
AC A0A1C4VLS6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Leader peptidase (Prepilin peptidase) / N-methyltransferase {ECO:0000313|EMBL:SCE84898.1};
GN ORFNames=GA0070607_2326 {ECO:0000313|EMBL:SCE84898.1};
OS Micromonospora coriariae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=285665 {ECO:0000313|EMBL:SCE84898.1, ECO:0000313|Proteomes:UP000198243};
RN [1] {ECO:0000313|EMBL:SCE84898.1, ECO:0000313|Proteomes:UP000198243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44875 {ECO:0000313|EMBL:SCE84898.1,
RC ECO:0000313|Proteomes:UP000198243};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A24 family.
CC {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
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DR EMBL; LT607412; SCE84898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4VLS6; -.
DR OrthoDB; 3388265at2; -.
DR Proteomes; UP000198243; Chromosome i.
DR GO; GO:0016020; C: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; IPR014032; Peptidase_A24A_bac.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
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; PF01478; Peptidase_A24; 1.
DR PRINTS; PR00864; PREPILNPTASE.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000313|EMBL:SCE84898.1};
KW Transferase {ECO:0000313|EMBL:SCE84898.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..239
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 28192 MW; 08333A0282FB2D47 CRC64;
MPLTGPPAAV PGQENPPDRL PAPSPSSAPR RPARPWLPAV LATVAVSPLL RLAVLRHAVP
SGTASRTGCD ACGAPVGLTR PWPALGPVGL CGRCRARVGP PPGTVELAAI VGLATVVLLA
LAGPPGAAPP ALAWWLGWTV PAVFVDLAVH RLPDRLTLPA AAGTWLLLGA AVLGGPEPGP
WLRAVTAGAG LAVLFAGSTL LLGRRGFGLG DAKLALSVGA LLGWYGWPFL LFGLLLAFGL
SALVSLGLLA ARRARWSTHL PFGPFLLLGT LGALLLAT
//
