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Database: UniProt
Entry: A0A0X8D0C6_9BACL
LinkDB: A0A0X8D0C6_9BACL
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ID   A0A0X8D0C6_9BACL        Unreviewed;       252 AA.
AC   A0A0X8D0C6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   16-JAN-2019, entry version 9.
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=ACH33_04130 {ECO:0000313|EMBL:AMA72116.1};
OS   Aneurinibacillus sp. XH2.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA72116.1, ECO:0000313|Proteomes:UP000065566};
RN   [1] {ECO:0000313|EMBL:AMA72116.1, ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|EMBL:AMA72116.1,
RC   ECO:0000313|Proteomes:UP000065566};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMA72116.1, ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|EMBL:AMA72116.1,
RC   ECO:0000313|Proteomes:UP000065566};
RA   Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT   "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT   Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao
RT   oilfield in China.";
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; CP014140; AMA72116.1; -; Genomic_DNA.
DR   RefSeq; WP_057897885.1; NZ_CP014140.1.
DR   EnsemblBacteria; AMA72116; AMA72116; ACH33_04130.
DR   KEGG; anx:ACH33_04130; -.
DR   KO; K02654; -.
DR   OrthoDB; 2046608at2; -.
DR   Proteomes; UP000065566; Chromosome.
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:UP000065566};
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:UP000065566};
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      6     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     74     94       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    100    120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    127    142       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    148    168       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    180    213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    225    248       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       11     92       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      105    209       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   252 AA;  28144 MW;  E29B53645193C14B CRC64;
     MDFAILLLVF LFGLLFGSFF NVVGLRVPQE QSLLAPPSHC PTCKKQLKPI DLIPILSYLI
     ARGKCRYCRA PISSVYPLIE LATGILFAAV YAVYDFTPVA WLYLLFISLL VIITVSDLAY
     RIIPDKVLLP FFLVFLVLRF FIHPDETYLS HLIGMVLGFT IFYIIAIVSG NGIGGGDIKL
     FAVVGLFLGY PLLLLTILLS TFFGAFYGVL LMIFRGAGRK TKVPFGPFIA LGALLALFKG
     YDLIAWYFSF FY
//
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