ID A0A1I6MFU0_9BACT Unreviewed; 324 AA.
AC A0A1I6MFU0;
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:SFS14478.1};
GN ORFNames=SAMN05421771_2542 {ECO:0000313|EMBL:SFS14478.1};
OS Granulicella pectinivorans.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=474950 {ECO:0000313|EMBL:SFS14478.1, ECO:0000313|Proteomes:UP000199024};
RN [1] {ECO:0000313|EMBL:SFS14478.1, ECO:0000313|Proteomes:UP000199024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21001 {ECO:0000313|EMBL:SFS14478.1,
RC ECO:0000313|Proteomes:UP000199024};
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; FOZL01000001; SFS14478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6MFU0; -.
DR STRING; 474950.SAMN05421771_2542; -.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000199024; 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:SFS14478.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199024};
KW Transferase {ECO:0000313|EMBL:SFS14478.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..106
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 139..280
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 324 AA; 35446 MW; 3662BE917D821376 CRC64;
MAEVYPAYTE VVLELWLITG CAFVIGLLLG SFLNVCIARL PYGESIVTPR SHCPACHHAI
RWYDNIPILS WLLLRARCRD CGQKISWQYP AVEIATGLWF MTAFAHAWDA WGMDQTGQVG
PWMAERLTID VIAGIATLIL GFLLIGLLVM DWQTHRLPDA FTLSGIAIGF FLVCTQAIFL
GPTEDQVLLH HKAPITAAMS VEKGNVFLTG PEALLGGRLV AIVGAALLLL AIRQAYKLLR
KRDGMGLGDI KLLAMIAAFL GFWPAILALF AGVLTASLYA ALLLVRGRAN RLTRLPFGSF
LAAGGLFSSL FGPALLDWYT SLFR
//
