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Database: UniProt
Entry: A0A1M3GW95_9PROT
LinkDB: A0A1M3GW95_9PROT
Original site: A0A1M3GW95_9PROT 
ID   A0A1M3GW95_9PROT        Unreviewed;       283 AA.
AC   A0A1M3GW95;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   10-APR-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=BGO60_03755 {ECO:0000313|EMBL:OJW47047.1};
OS   Thiobacillus sp. 65-1059.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1895860 {ECO:0000313|EMBL:OJW47047.1, ECO:0000313|Proteomes:UP000184230};
RN   [1] {ECO:0000313|EMBL:OJW47047.1, ECO:0000313|Proteomes:UP000184230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65-1059 {ECO:0000313|EMBL:OJW47047.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T.,
RA   Anantharaman K., Tringe S., Hettich R.L., Harrison S.T.,
RA   Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process
RT   performance in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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}.
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:OJW47047.1}.
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DR   EMBL; MKUE01000105; OJW47047.1; -; Genomic_DNA.
DR   Proteomes; UP000184230; 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:UP000184230};
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     12     30       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    126    143       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    155    172       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    178    196       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    228    247       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    259    280       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       17    122       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      133    241       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   283 AA;  30723 MW;  7AB50D4377235CFC CRC64;
     MALLHAEPAL FTGLVFLFGL LVGSFLNVAI HRLPRMMEAE WHAQCAELRG EALPDAPRYN
     LWLPRSACPQ CGHRITALEN IPLLSWLWLR GRCSACRAPI GARYPLVELL TALLSAAVAW
     KWGASVQTAG ALLMVWMLIA LAFIDLDTTL LPDSLTLPLL WLGLLFNLGG HFSSLPDAVV
     GAMAGYLVLW LVYWLFKLAT GKDGMGYGDF KLLAAIGAWL GWQMLPVTLL LSSVVGAAVG
     IAMIVLVKHD RRVPIPFGPY LAGGGLVALF FGADLTQAYL GQF
//
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