ID A0A0G0RHV6_9BACT Unreviewed; 283 AA.
AC A0A0G0RHV6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Type 4 prepilin-like protein leader peptide-processing enzyme {ECO:0000313|EMBL:KKR52269.1};
GN ORFNames=UT89_C0002G0070 {ECO:0000313|EMBL:KKR52269.1};
OS Parcubacteria group bacterium GW2011_GWE1_40_20.
OC Bacteria.
OX NCBI_TaxID=1618946 {ECO:0000313|EMBL:KKR52269.1, ECO:0000313|Proteomes:UP000034131};
RN [1] {ECO:0000313|EMBL:KKR52269.1, ECO:0000313|Proteomes:UP000034131}
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:KKR52269.1}.
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DR EMBL; LBYN01000002; KKR52269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0RHV6; -.
DR Proteomes; UP000034131; 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 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..93
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 120..231
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 283 AA; 31988 MW; 4526F7404FC03D2F CRC64;
MDFLTYVYIF ILGTLIGSFI NVVAMRFNTG LSIYNSRSKC FSCSRELAWY ELIPIFSYFF
LLGKCRSCKS GISLQYPFVE LLTGLVFVAI ALRQVGLWST YSAFDNGLLL SILFFVFYAV
VFSLLIVIML YDIRHKIIPN ALVYTLIVLS VVKLLSFLYL KGFTLSVADW FDLGTPFLLF
IPFALLWFMS GGKWIGFGDA KLVFGIGALT GFVFGVGSIV LAFWIGAVWS IGLMIYSKYN
KGHKVTLRTE IPFAPFLILS TIIVFVTRID VVGLQNLIEL FYQ
//
