ID B4SEK5_PELPB Unreviewed; 292 AA.
AC B4SEK5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Peptidase A24A prepilin type IV {ECO:0000313|EMBL:ACF43097.1};
GN OrderedLocusNames=Ppha_0807 {ECO:0000313|EMBL:ACF43097.1};
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF43097.1, ECO:0000313|Proteomes:UP000002724};
RN [1] {ECO:0000313|EMBL:ACF43097.1, ECO:0000313|Proteomes:UP000002724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A24 family.
CC {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
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DR EMBL; CP001110; ACF43097.1; -; Genomic_DNA.
DR AlphaFoldDB; B4SEK5; -.
DR STRING; 324925.Ppha_0807; -.
DR KEGG; pph:Ppha_0807; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_083001_0_0_10; -.
DR OrthoDB; 598067at2; -.
DR Proteomes; UP000002724; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR Gene3D; 1.20.120.1220; -; 1.
DR InterPro; IPR014032; Peptidase_A24A_bac.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
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; PF01478; Peptidase_A24; 1.
DR PRINTS; PR00864; PREPILNPTASE.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002724};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..203
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 292 AA; 31589 MW; 4DAD9C8B0E904000 CRC64;
MNISSPLQIL WGQLPWLLAG AGLGLWLVPL ARIIPRKVLQ SAKVPLNAWQ GPGGGLEQPI
PAARRIWVPM VNTSMWAYVA NSVSHPAFQA VLLWACLAST LLLLALIDWD STLLPDWVVL
PLGVVGLASS YAGFTPHSLF VSALSAAVVL GLLGGLAWLF RRIKGESGIG GGDLKLLAAL
ATWWGIVGVL YIVLWASVVT VLWYVVWRRF KGLGPQAEWP FGPAIVVAAL AWGLQTAYLP
TQLDADSYHG PKRTALPTLQ EQVESECQAL QTYSARVIEA AVRIETEGYA IR
//
