ID A0A0H4P365_9BACI Unreviewed; 252 AA.
AC A0A0H4P365;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=N-methyltransferase {ECO:0000313|EMBL:AKP48264.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:AKP48264.1};
DE EC=3.4.23.43 {ECO:0000313|EMBL:AKP48264.1};
GN ORFNames=BSM4216_3058 {ECO:0000313|EMBL:AKP48264.1};
OS Bacillus smithii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP48264.1, ECO:0000313|Proteomes:UP000036353};
RN [1] {ECO:0000313|EMBL:AKP48264.1, ECO:0000313|Proteomes:UP000036353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP48264.1,
RC ECO:0000313|Proteomes:UP000036353};
RA Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA van Kranenburg R.;
RT "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT 4216T.";
RL Submitted (JUL-2015) 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; CP012024; AKP48264.1; -; Genomic_DNA.
DR RefSeq; WP_048623905.1; NZ_CP012024.1.
DR AlphaFoldDB; A0A0H4P365; -.
DR STRING; 1479.BSM4216_3058; -.
DR KEGG; bsm:BSM4216_3058; -.
DR eggNOG; COG1989; Bacteria.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000036353; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:AKP48264.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000313|EMBL:AKP48264.1};
KW Transferase {ECO:0000313|EMBL:AKP48264.1};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..94
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 104..208
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 252 AA; 28555 MW; 710A5736C34B9B6E CRC64;
MNTFWTVYFA VIGLVFGSFF NVVGLRVPNH ESIVFPSSHC PYCHHKLRWF ENIPLFSFFF
LKGKCRSCKR KISWIYPIFE AVTGVLFAFS FYQFGWSMNL VMACLFTSLL VVITVSDLAY
MVIPDKILLP FMILFIVIRL LSPTVPWWSS WAGAVIGFGL LFLIAVVTNG AMGGGDIKLY
FVIGLILGLE KTLLSFFLAC LFGSLFGLIF LFKGKFKKGK PVPFGPFIAA GAILAFFYGQ
DMIDFYIRTM WS
//
