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Database: UniProt
Entry: A0A0H2LVN7_VARPD
LinkDB: A0A0H2LVN7_VARPD
Original site: A0A0H2LVN7_VARPD 
ID   A0A0H2LVN7_VARPD        Unreviewed;       321 AA.
AC   A0A0H2LVN7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-DEC-2018, entry version 11.
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   Name=outO {ECO:0000313|EMBL:KLN53786.1};
GN   ORFNames=VPARA_51180 {ECO:0000313|EMBL:KLN53786.1};
OS   Variovorax paradoxus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN53786.1, ECO:0000313|Proteomes:UP000035170};
RN   [1] {ECO:0000313|EMBL:KLN53786.1, ECO:0000313|Proteomes:UP000035170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBEA6 {ECO:0000313|EMBL:KLN53786.1,
RC   ECO:0000313|Proteomes:UP000035170};
RA   Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA   Daniel R.;
RT   "Genome sequence of Variovorax paradoxus TBEA6.";
RL   Submitted (MAR-2015) 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:KLN53786.1}.
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DR   EMBL; JZWI01000030; KLN53786.1; -; Genomic_DNA.
DR   RefSeq; WP_047786517.1; NZ_JZWI01000030.1.
DR   EnsemblBacteria; KLN53786; KLN53786; VPARA_51180.
DR   PATRIC; fig|34073.19.peg.5239; -.
DR   Proteomes; UP000035170; 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:UP000035170};
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:UP000035170};
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     28       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    157    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    188    221       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    241    271       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    283    302       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       14    150       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      161    270       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   321 AA;  34342 MW;  6C6F968D6E69C358 CRC64;
     MLVSQEFDAA FAGVLGLLVG SFLNVVIYRT PVMMYRGWLA DAVANLMSSK DVPSLWTLVF
     GAKAQPPAGL EAAADKAAVA IEALPPFDLT RPASRCGACG HKIRWYQNIP VLSYLVLRGR
     CAACKTPISP RYPLVELVTG ALFALCAYRF GLTPTGALWA AFAAFLICQF LIDFDTQFLP
     DALNYPLLWL GLIGAAMGWT GTALSSAVWG AVFGYLSLWL VYHGYRLVTG KEGMGYGDFK
     LLAALGAWLG ADYLIAIILV SSLVGAVIGL TLRLVGKLAH KDIPMAFGPF LAGAGLVCLV
     AGPELVRQWI PFAFPLGAFA R
//
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