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Database: UniProt
Entry: K0CJP1_ALCDB
LinkDB: K0CJP1_ALCDB
Original site: K0CJP1_ALCDB 
ID   K0CJP1_ALCDB            Unreviewed;       287 AA.
AC   K0CJP1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   10-APR-2019, entry version 34.
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:AFT71741.1};
GN   OrderedLocusNames=B5T_03474 {ECO:0000313|EMBL:AFT71741.1};
OS   Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / B-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71741.1, ECO:0000313|Proteomes:UP000006286};
RN   [1] {ECO:0000313|EMBL:AFT71741.1, ECO:0000313|Proteomes:UP000006286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC   {ECO:0000313|Proteomes:UP000006286};
RX   PubMed=23144414; DOI=10.1128/JB.01813-12;
RA   Lai Q., Li W., Shao Z.;
RT   "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL   J. Bacteriol. 194:6674-6674(2012).
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; CP003466; AFT71741.1; -; Genomic_DNA.
DR   RefSeq; WP_014995802.1; NC_018691.1.
DR   STRING; 930169.B5T_03474; -.
DR   MEROPS; A24.001; -.
DR   EnsemblBacteria; AFT71741; AFT71741; B5T_03474.
DR   KEGG; adi:B5T_03474; -.
DR   PATRIC; fig|930169.3.peg.3434; -.
DR   KO; K02654; -.
DR   OMA; VFWLFKL; -.
DR   OrthoDB; 2046608at2; -.
DR   BioCyc; ADIE930169:G1HAU-3481-MONOMER; -.
DR   Proteomes; UP000006286; 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:UP000006286};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:AFT71741.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:AFT71741.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     31       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    129    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    159    177       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    183    202       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    214    247       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    259    284       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       18    123       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      136    243       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   287 AA;  31468 MW;  F25FC85A06074DF5 CRC64;
     MFSFLADQPA LLIIFCTVFG LLVGSFLNVV IHRVPRMMER TWRREAQEVL ELPIEETSPY
     NLVVPRSRCP HCDHAIRWHE NIPVISWLLL KGRCSACGQG ISARYPLIEL LSALIAAVCA
     WQFGYGSWLV FVLFASFTLL ALAAIDLDTT LLPDAMTFPL LWAGLLAALL GISPVSLPDA
     VVGAMAGYLS LWSLYWVFKL VTGKEGMGYG DFKLLAALGA WLGWQYLPLV ILLSSVVGLV
     FAIGMMARGG LKKGQGIPFG PYLAIAGWIA LLWGDTIVGA YLGLFQF
//
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