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Database: UniProt
Entry: U5QIJ5_9CYAN
LinkDB: U5QIJ5_9CYAN
Original site: U5QIJ5_9CYAN 
ID   U5QIJ5_9CYAN            Unreviewed;       275 AA.
AC   U5QIJ5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   10-APR-2019, entry version 23.
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:AGY57480.1};
GN   ORFNames=GKIL_1234 {ECO:0000313|EMBL:AGY57480.1};
OS   Gloeobacter kilaueensis JS1.
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales;
OC   Gloeobacteraceae; Gloeobacter.
OX   NCBI_TaxID=1183438 {ECO:0000313|EMBL:AGY57480.1, ECO:0000313|Proteomes:UP000017396};
RN   [1] {ECO:0000313|EMBL:AGY57480.1, ECO:0000313|Proteomes:UP000017396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS {ECO:0000313|Proteomes:UP000017396};
RX   PubMed=24194836; DOI=10.1371/journal.pone.0076376;
RA   Saw J.H., Schatz M., Brown M.V., Kunkel D.D., Foster J.S., Shick H.,
RA   Christensen S., Hou S., Wan X., Donachie S.P.;
RT   "Cultivation and Complete Genome Sequencing of Gloeobacter kilaueensis
RT   sp. nov., from a Lava Cave in Kilauea Caldera, Hawai'i.";
RL   PLoS ONE 8:E76376-E76376(2013).
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; CP003587; AGY57480.1; -; Genomic_DNA.
DR   RefSeq; WP_023172568.1; NC_022600.1.
DR   STRING; 1183438.GKIL_1234; -.
DR   EnsemblBacteria; AGY57480; AGY57480; GKIL_1234.
DR   KEGG; glj:GKIL_1234; -.
DR   PATRIC; fig|1183438.3.peg.1217; -.
DR   KO; K02654; -.
DR   OrthoDB; 2046608at2; -.
DR   BioCyc; GKIL1183438:G1HLA-1218-MONOMER; -.
DR   Proteomes; UP000017396; 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:UP000017396};
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:UP000017396};
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     77     98       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    110    128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    140    158       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    170    188       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    218    237       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    249    268       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       15     97       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      116    232       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   275 AA;  29079 MW;  96D9C059E6782CDE CRC64;
     MRGPFFLLAI GYWAILGAAA GSFANVVADR LPAGRSLLWP PSHCAQCGRV LRPLENVPVL
     GWLWLRGRCR SCGAAIPVRY AIVEALGALL FGLLAWHLGA RFTPVSMVQT AFWGSFLTLL
     LALSLIDLDR LELPGELTSA GIVLGLGFRT FFPIWATGSW PAGPPGLVDA LYGLILGIGL
     FDIVSYLGEK MLGKEAMGGG DAVLAAMIGV WLGWKLLLVA LFVGFCLGAV GGILGLATGH
     LKRDEPLPFG PFLALGGVGG LLFGQSWLTG YLSLF
//
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