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Database: UniProt
Entry: B5WM93_9BURK
LinkDB: B5WM93_9BURK
Original site: B5WM93_9BURK 
ID   B5WM93_9BURK            Unreviewed;       313 AA.
AC   B5WM93;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   16-JAN-2019, entry version 40.
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   ORFNames=BH160DRAFT_4196 {ECO:0000313|EMBL:EEA00533.1};
OS   Burkholderia sp. H160.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=516466 {ECO:0000313|EMBL:EEA00533.1, ECO:0000313|Proteomes:UP000004534};
RN   [1] {ECO:0000313|EMBL:EEA00533.1, ECO:0000313|Proteomes:UP000004534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H160 {ECO:0000313|EMBL:EEA00533.1,
RC   ECO:0000313|Proteomes:UP000004534};
RX   PubMed=23209196; DOI=10.1128/JB.01756-12;
RA   Ormeno-Orrillo E., Rogel M.A., Chueire L.M., Tiedje J.M.,
RA   Martinez-Romero E., Hungria M.;
RT   "Genome Sequences of Burkholderia sp. Strains CCGE1002 and H160,
RT   Isolated from Legume Nodules in Mexico and Brazil.";
RL   J. Bacteriol. 194:6927-6927(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEA00533.1}.
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DR   EMBL; ABYL01000064; EEA00533.1; -; Genomic_DNA.
DR   MEROPS; A24.A10; -.
DR   EnsemblBacteria; EEA00533; EEA00533; BH160DRAFT_4196.
DR   Proteomes; UP000004534; 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:UP000004534};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:EEA00533.1}; 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     37     59       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    144    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    207    228       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    248    277       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    289    311       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       46    153       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      166    273       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   313 AA;  33101 MW;  B3161D91BFB039E8 CRC64;
     MQAPLPLVSQ TSSNLLAGLL PGRFASDIGL GFASLPAGVQ IAFAIVLGLV IGSFLNVVVH
     RLPIMLERAW RDEISEATDE PQPDDGLPAR YNLWVPRSAC PHCGHVLSAW ENLPVLSYVL
     LRGRCSACGT HISSRYPLLE IASAVFAAGA LITFGPNLTA LAAFGLCATL LAMSAIDIDT
     HLLPDSLTLP LLWAGLIVNF NGMFTNLHGA VLGAIFGYLV LWAVHWVFKL VRGVEGMGYG
     DFKLLAALGA WLGWPALPQI VLIAAVAGAV IGLAATWRGR MRFEEPLPFG PFLAAGGALT
     LFVGTPLYLA LGG
//
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