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Database: UniProt
Entry: A0A158HA78_9BURK
LinkDB: A0A158HA78_9BURK
Original site: A0A158HA78_9BURK 
ID   A0A158HA78_9BURK        Unreviewed;       297 AA.
AC   A0A158HA78;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   16-JAN-2019, entry version 6.
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=AWB65_03121 {ECO:0000313|EMBL:SAL41047.1};
OS   Caballeronia humi.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL41047.1, ECO:0000313|Proteomes:UP000054977};
RN   [1] {ECO:0000313|EMBL:SAL41047.1, ECO:0000313|Proteomes:UP000054977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL41047.1};
RA   Oliw E.H.;
RL   Submitted (JAN-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; FCNW02000014; SAL41047.1; -; Genomic_DNA.
DR   Proteomes; UP000054977; 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:UP000054977};
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   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     20     46       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    142    160       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    166    184       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    196    216       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    236    262       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    274    296       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       33    138       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      150    258       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   297 AA;  32104 MW;  4D00D5C9D6F94A89 CRC64;
     MQPSFEPYVA RSSLFTQAFA ALPAAAQYGF AIVFGLVIGS FLTVVVHRLP IMLERAWRAE
     IDAETTGDAA PAERYNLAVP RSACPHCGHI LRAWENIPVV SYMLLRGRCA KCGASVSARY
     PLIELATALF AAASLYAFGP DWLALAAFGL CATLLATSLI DFDTRYLPDS LTLPLLWAGL
     IVNLSDGGFV QLHDAVIGAI GGYLFLWCVY WIFRLVRGVE GMGYGDFKLL AALGAWLGWM
     ALPQIVLVSA IAGALVGLVA TWRGRMRFEE PLPFGPFLAI GGVLTLYFGT PLYGLFG
//
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