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Database: UniProt
Entry: A0A157SD80_9BORD
LinkDB: A0A157SD80_9BORD
Original site: A0A157SD80_9BORD 
ID   A0A157SD80_9BORD        Unreviewed;       289 AA.
AC   A0A157SD80;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-DEC-2018, entry version 8.
DE   RecName: Full=Type 4 prepilin-like proteins leader peptide-processing enzyme {ECO:0000256|RuleBase:RU003794};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU003794};
DE            EC=3.4.23.43 {ECO:0000256|RuleBase:RU003794};
GN   Name=outO {ECO:0000313|EMBL:SAI67856.1};
GN   ORFNames=SAMEA3906486_01757 {ECO:0000313|EMBL:SAI67856.1};
OS   Bordetella ansorpii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI67856.1, ECO:0000313|Proteomes:UP000076848};
RN   [1] {ECO:0000313|EMBL:SAI67856.1, ECO:0000313|Proteomes:UP000076848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050680373 {ECO:0000313|EMBL:SAI67856.1,
RC   ECO:0000313|Proteomes:UP000076848};
RG   Pathogen Informatics;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates
CC       the N-terminal (generally Phe) residue.
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Typically cleaves a -Gly-|-Phe- bond to release an N-
CC         terminal, basic peptide of 5-8 residues from type IV prepilin,
CC         and then N-methylates the new N-terminal amino group, the methyl
CC         donor being S-adenosyl-L-methionine.; EC=3.4.23.43;
CC         Evidence={ECO:0000256|RuleBase:RU003794};
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU003794}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003794}.
CC   -!- SIMILARITY: Belongs to the peptidase A24 family.
CC       {ECO:0000256|RuleBase:RU003793}.
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DR   EMBL; FKIF01000002; SAI67856.1; -; Genomic_DNA.
DR   RefSeq; WP_066125700.1; NZ_FKIF01000002.1.
DR   EnsemblBacteria; SAI67856; SAI67856; SAMEA3906486_01757.
DR   Proteomes; UP000076848; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR010627; Pept_A24A_N.
DR   InterPro; IPR014032; Peptidase_A24A_bac.
DR   InterPro; IPR000045; Prepilin_IV_endopep_pep.
DR   Pfam; PF06750; DiS_P_DiS; 1.
DR   Pfam; PF01478; Peptidase_A24; 1.
DR   PRINTS; PR00864; PREPILNPTASE.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076848};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076848};
KW   Transferase {ECO:0000256|RuleBase:RU003794};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    133    150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    181    202       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    261    279       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       18    128       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      140    247       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   289 AA;  30302 MW;  A4B8DD391040E119 CRC64;
     MWHMYSLDPG LAVLLAALLG LAVSGPLGAV AHRLPRIMER EWQAALRQEQ AAAESPAESD
     AGQPYGLLRP GWHCPSCEAP VRGWRAMPLV GWLALRGKCA GCRAPIGRRY PAFELAMAAL
     FAACAWRFGP TPMALCAMGL VGALLVLGWI DTETGLLPDA ITLPLAWAGL LVNLGDGLAP
     LSLAVVGAVT GYLVLWSVFH VFKLVTGREG MGYGDFKLMA ALGAWLGVAA LPWLLLGASL
     AGVIVGLGLR VAGRVEQGQP LPFGPYLAAG GILMLLAAGQ PPWLAVFGR
//
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