GenomeNet

Database: UniProt
Entry: G0ADX4_COLFT
LinkDB: G0ADX4_COLFT
Original site: G0ADX4_COLFT 
ID   G0ADX4_COLFT            Unreviewed;       288 AA.
AC   G0ADX4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   16-JAN-2019, entry version 38.
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=pilD {ECO:0000313|EMBL:AEK63747.1};
GN   OrderedLocusNames=CFU_3924 {ECO:0000313|EMBL:AEK63747.1};
OS   Collimonas fungivorans (strain Ter331).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK63747.1, ECO:0000313|Proteomes:UP000008392};
RN   [1] {ECO:0000313|EMBL:AEK63747.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63747.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA   Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT   "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT   expression of ribosomal RNA genes by large-insert library fluorescent
RT   in situ hybridization (LIL-FISH).";
RL   Environ. Microbiol. 6:990-998(2004).
RN   [2] {ECO:0000313|EMBL:AEK63747.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63747.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA   Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT   "Genomic flank-sequencing of plasposon insertion sites for rapid
RT   identification of functional genes.";
RL   J. Microbiol. Methods 66:276-285(2006).
RN   [3] {ECO:0000313|EMBL:AEK63747.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63747.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA   Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA   Leveau J.H.;
RT   "Identification and characterization of genes underlying chitinolysis
RT   in Collimonas fungivorans Ter331.";
RL   FEMS Microbiol. Ecol. 66:123-135(2008).
RN   [4] {ECO:0000313|EMBL:AEK63747.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63747.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA   Leveau J.H., Uroz S., de Boer W.;
RT   "The bacterial genus Collimonas: mycophagy, weathering and other
RT   adaptive solutions to life in oligotrophic soil environments.";
RL   Environ. Microbiol. 12:281-292(2010).
RN   [5] {ECO:0000313|EMBL:AEK63747.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63747.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA   Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA   van den Berg M., Leveau J.H.;
RT   "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT   Collimonas fungivorans versus Aspergillus niger.";
RL   ISME J. 5:1494-1504(2011).
RN   [6] {ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA   Leveau J.H.;
RT   "Complete sequence of Collimonas fungivorans Ter331.";
RL   Submitted (MAY-2011) 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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002745; AEK63747.1; -; Genomic_DNA.
DR   RefSeq; WP_014007899.1; NC_015856.1.
DR   STRING; 1005048.CFU_3924; -.
DR   MEROPS; A24.001; -.
DR   EnsemblBacteria; AEK63747; AEK63747; CFU_3924.
DR   KEGG; cfu:CFU_3924; -.
DR   eggNOG; ENOG4105EHH; Bacteria.
DR   eggNOG; COG1989; LUCA.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   BioCyc; CFUN1005048:G1GZG-4155-MONOMER; -.
DR   Proteomes; UP000008392; 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:UP000008392};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:AEK63747.1}; 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   Reference proteome {ECO:0000313|Proteomes:UP000008392};
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     34       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    130    148       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    177       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    183    200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    232    251       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    263    286       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       21    126       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      136    245       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   288 AA;  31202 MW;  1A53082DFED630B9 CRC64;
     MQDGIFFLAA GSLLPTVLAA VFGLLIGSFL NVVIHRLPIM MQRESDNYVA HESGKPLPHT
     ERYNLVVPRS ACTQCKHQIG ALENVPILSY LALRGKCAAC KTPISIRYPL VEALTGALSA
     LLIWHFGSGW VGLATLVLLY LLIAMTFIDA DTQLLPDDLT LPLLWIGLLL NLSGLFVPLQ
     DAVIGAAAGY LSLWAIYWAF KLLTGKEGMG YGDFKLLAAL GAWLGWKMLP IIILFSSLVG
     AVVGIILIVF ARRGRDKPIP FGPYLAAAGL LALLYGQTIL ETYFGFAT
//
DBGET integrated database retrieval system