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Database: UniProt
Entry: A0A261SWA9_9BORD
LinkDB: A0A261SWA9_9BORD
Original site: A0A261SWA9_9BORD 
ID   A0A261SWA9_9BORD        Unreviewed;       271 AA.
AC   A0A261SWA9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Prepilin peptidase {ECO:0000313|EMBL:OZI41150.1};
GN   ORFNames=CEG14_02805 {ECO:0000313|EMBL:OZI41150.1};
OS   Bordetella genomosp. 1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395607 {ECO:0000313|EMBL:OZI41150.1, ECO:0000313|Proteomes:UP000217005};
RN   [1] {ECO:0000313|EMBL:OZI41150.1, ECO:0000313|Proteomes:UP000217005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17610 {ECO:0000313|EMBL:OZI41150.1,
RC   ECO:0000313|Proteomes:UP000217005};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|ARBA:ARBA00005801, ECO:0000256|RuleBase:RU003793}.
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:OZI41150.1}.
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DR   EMBL; NEVL01000001; OZI41150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SWA9; -.
DR   OrthoDB; 9789291at2; -.
DR   Proteomes; UP000217005; Unassembled WGS sequence.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..226
FT                   /note="Prepilin type IV endopeptidase peptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01478"
SQ   SEQUENCE   271 AA;  28748 MW;  01613A8184D776AE CRC64;
     MWHEWHWSPA WALALAALAG LAVGGCLTWV VYRLPVALRR GWRGGPPMTP PRPLRGERVR
     AVPLAGWWLA RGGRIGLRAR ARRQGFGPGW ALPLAELACA VLFALCVWRF GVTLAALAAM
     VLCAALLTLA WIDLRLGLLP DVLTLPLAWA GLLVNLGTGF ATLPQAVLGA VAGYLFLWLV
     FHLFRLCTGR DGMGYGDFKL SAALGAWLGL ADLPTILLLA SLGGVLAGWG LRLAGRVGRG
     EPLPFAPFLA SAGLAALFLQ EHGAAAPGLL H
//
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