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Database: UniProt
Entry: A4JBB0_BURVG
LinkDB: A4JBB0_BURVG
Original site: A4JBB0_BURVG 
ID   A4JBB0_BURVG            Unreviewed;       303 AA.
AC   A4JBB0;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
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   OrderedLocusNames=Bcep1808_0551 {ECO:0000313|EMBL:ABO53563.1};
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia
OS   cepacia (strain R1808)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO53563.1, ECO:0000313|Proteomes:UP000002287};
RN   [1] {ECO:0000313|Proteomes:UP000002287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) 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; CP000614; ABO53563.1; -; Genomic_DNA.
DR   STRING; 269482.Bcep1808_0551; -.
DR   MEROPS; A24.A10; -.
DR   EnsemblBacteria; ABO53563; ABO53563; Bcep1808_0551.
DR   KEGG; bvi:Bcep1808_0551; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   HOGENOM; HOG000248584; -.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   BioCyc; BVIE269482:GJNA-557-MONOMER; -.
DR   Proteomes; UP000002287; Chromosome 1.
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:UP000002287};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:ABO53563.1}; 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   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     26     47       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    122    143       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    149    166       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    178    194       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    250    267       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    279    301       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       34    141       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      156    263       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   303 AA;  32200 MW;  16381614DC606AB4 CRC64;
     MTRAPMFPVP DSPAGTLLAL ALLPPAVQYA FAVVIGLCVG SFINVVAHRV PVMMQRAWRA
     EIAEATGNAD AAPDDGYPQR YDLWRPRSAC PHCGHVLRAW ENVPLLSYVM LRGRCRQCGH
     AIGIRYPLVE LAGALLAAGS LAAFGPTGAA IAAFGLCAAL LAMSAIDIRT GYLPDSMTLP
     LLWAGLALNL AGMFTSLQSA VIGAMSGYLF LWSIYWLFRW LRGIEGIGFG DLKLLAALGA
     WMGWAALPQV VLFAAVTGAI VGLVATWRGR MRFEEPIPFG PFLAAGGVAT LFFGTPFYSA
     LGG
//
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