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Database: UniProt
Entry: A0A075R307_BRELA
LinkDB: A0A075R307_BRELA
Original site: A0A075R307_BRELA 
ID   A0A075R307_BRELA        Unreviewed;       172 AA.
AC   A0A075R307;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative Flp pilus assembly protein {ECO:0000313|EMBL:AIG25578.1};
GN   ORFNames=BRLA_c012380 {ECO:0000313|EMBL:AIG25578.1};
OS   Brevibacillus laterosporus LMG 15441.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG25578.1, ECO:0000313|Proteomes:UP000005850};
RN   [1] {ECO:0000313|EMBL:AIG25578.1, ECO:0000313|Proteomes:UP000005850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG25578.1,
RC   ECO:0000313|Proteomes:UP000005850};
RX   PubMed=21914864; DOI=10.1128/JB.05696-11;
RA   Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT   "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT   invertebrates.";
RL   J. Bacteriol. 193:5535-5536(2011).
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
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DR   EMBL; CP007806; AIG25578.1; -; Genomic_DNA.
DR   RefSeq; WP_041751980.1; NZ_CP007806.1.
DR   AlphaFoldDB; A0A075R307; -.
DR   STRING; 1042163.BRLA_c012380; -.
DR   KEGG; blr:BRLA_c012380; -.
DR   eggNOG; COG1989; Bacteria.
DR   HOGENOM; CLU_057101_8_0_9; -.
DR   Proteomes; UP000005850; 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:UP000005850};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..129
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   172 AA;  18984 MW;  7E0F241C46F41B26 CRC64;
     MMLQWGWPII LGEEAGIERL ICWICGGLLG VICFLDIRKR LIPNSIVLPA TFTFLCVRVI
     HPLEKETFTT HMLAMLLAFV LLYVTAIVTK GGLGGGDIKL AALLGLIVGR TYIISLLLVA
     GISTIALAIL LARQPRIRKE GIPFACCLTI GWLFTYVGRM DVLHVYAIFF LP
//
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