ID   A0A1H0S7Z3_9MICC        Unreviewed;       233 AA.
AC   A0A1H0S7Z3;
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:SDP37765.1};
GN   ORFNames=SAMN04487914_109115 {ECO:0000313|EMBL:SDP37765.1};
OS   Arthrobacter sp. ok909.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1761746 {ECO:0000313|EMBL:SDP37765.1, ECO:0000313|Proteomes:UP000199538};
RN   [1] {ECO:0000313|EMBL:SDP37765.1, ECO:0000313|Proteomes:UP000199538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK909 {ECO:0000313|EMBL:SDP37765.1,
RC   ECO:0000313|Proteomes:UP000199538};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNJS01000009; SDP37765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0S7Z3; -.
DR   STRING; 1761746.SAMN04487914_109115; -.
DR   Proteomes; UP000199538; Unassembled WGS sequence.
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:SDP37765.1};
KW   Transferase {ECO:0000313|EMBL:SDP37765.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          90..200
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   233 AA;  23904 MW;  70E2F52961B9E7D2 CRC64;
     MSDPAAAGTA SLLFAQPLGS FTDVLFIAGV GLAGACLSLL AEFLIRRALP RLGALPTLRT
     RITTAAVTFA LSALLAWRLG PSPELPAYLL LAVAGVQLAR IDLIHHLLPN RMVLPLLGAG
     LMLLGAAAGV SGEAGNLLRG VAGGLILFIS YLILALTSRN GLGMGDVKLA APLGLYLGYL
     GWSHLFYGGA LGFVTGGIVS VVIVLKNRGN KPKEVAYGPS MLAAGLAVIL LFP
//