ID A0A1Q2HM49_9BACT Unreviewed; 400 AA.
AC A0A1Q2HM49;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Leader peptidase PppA {ECO:0000313|EMBL:AQQ08286.1};
GN Name=pppA {ECO:0000313|EMBL:AQQ08286.1};
GN ORFNames=L21SP3_00062 {ECO:0000313|EMBL:AQQ08286.1};
OS Sedimentisphaera cyanobacteriorum.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Sedimentisphaeraceae; Sedimentisphaera.
OX NCBI_TaxID=1940790 {ECO:0000313|EMBL:AQQ08286.1, ECO:0000313|Proteomes:UP000188273};
RN [1] {ECO:0000313|Proteomes:UP000188273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D3 {ECO:0000313|Proteomes:UP000188273};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) 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; CP019633; AQQ08286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2HM49; -.
DR STRING; 1940790.L21SP3_00062; -.
DR KEGG; pbu:L21SP3_00062; -.
DR Proteomes; UP000188273; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..105
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 284..356
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 400 AA; 43911 MW; 04B30764E9D9AE39 CRC64;
MICSWKLICG DWLVTAGIML YMFVVGACAG SFLNVVIHRL PRGVFLSERR SFCTSCGKFI
PLRENLPLIS WFMLRGKCRG CGARISPRYV IIEFLTAAFL ALLYYFYFSA GTISFSNSQT
NFVDFFAGGW WLYLSHAVLF CCLIAASAID LEMYLIPMSL CIFAAIFGLL TAAAAPFFID
YWQITEFQIF PYSSLRFSGL IAGGGAGILA ANILLDAGII KPSYEGLELE AEPAETQENI
SENPGFNDRR EVLKEFVFLI PIVLFALAGW KLLTPLQSWQ NLAANPHLSC LLGAAGGYLT
GAGIVWLTRI LGTLAFGREA MGLGDVHLMG AIGVFCGALP SIIIFFAAPF FGLAFTVIQL
ITKKNKEIPY GPFLSLAAVF VIIFREAVFE WLSNTMGFAG
//
