ID A0A0G1MDQ5_9BACT Unreviewed; 278 AA.
AC A0A0G1MDQ5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative type IV leader peptidase/N-methyltransferase {ECO:0000313|EMBL:KKT79022.1};
GN ORFNames=UW75_C0028G0003 {ECO:0000313|EMBL:KKT79022.1};
OS Parcubacteria group bacterium GW2011_GWF2_44_8.
OC Bacteria.
OX NCBI_TaxID=1618971 {ECO:0000313|EMBL:KKT79022.1, ECO:0000313|Proteomes:UP000034896};
RN [1] {ECO:0000313|EMBL:KKT79022.1, ECO:0000313|Proteomes:UP000034896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKT79022.1}.
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DR EMBL; LCJN01000028; KKT79022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1MDQ5; -.
DR PATRIC; fig|1618971.3.peg.307; -.
DR Proteomes; UP000034896; 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:KKT79022.1};
KW Transferase {ECO:0000313|EMBL:KKT79022.1};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..98
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 110..220
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 278 AA; 31083 MW; ABC8CD95355FAEDD CRC64;
MFYLTGLPFG LFVTIFFVFG VIIGSFLNVY LYRLHTGKSL MGSSHCLSCG NPLRAYELVP
ILSYLALRGR CRKCNSYIPK RYLLVELLTG LLFVGVALVA ADIMSLLHLL FFVSVLVVIA
VYDIYHLVIP DELVGSLMVT AMTYKFYLLI IGSPVQAFWF DVVTALIASL FLLSLWRVSK
GTWIGFGDVK LVIPLALWVG YQAAFSMVVL AFWIGAVVGV LSILSHNIYR RGQPHLRFLP
QELTMKSAIP FAPFLILGYL TVLFFGIDVI SLLSYVPQ
//
