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Database: UniProt
Entry: A0A0M9GDN2_9PSED
LinkDB: A0A0M9GDN2_9PSED
Original site: A0A0M9GDN2_9PSED 
ID   A0A0M9GDN2_9PSED        Unreviewed;       290 AA.
AC   A0A0M9GDN2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   13-FEB-2019, entry version 9.
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=PF66_05141 {ECO:0000313|EMBL:KPA88369.1};
OS   Pseudomonas fuscovaginae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA88369.1, ECO:0000313|Proteomes:UP000037931};
RN   [1] {ECO:0000313|EMBL:KPA88369.1, ECO:0000313|Proteomes:UP000037931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA88369.1,
RC   ECO:0000313|Proteomes:UP000037931};
RX   PubMed=26422147;
RA   Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S.,
RA   Mauleon R., Cruz C.V., Oliva R.;
RT   "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT   Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL   PLoS ONE 10:E0139256-E0139256(2015).
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:KPA88369.1}.
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DR   EMBL; JSYZ01000020; KPA88369.1; -; Genomic_DNA.
DR   RefSeq; WP_054058989.1; NZ_JTBY01000133.1.
DR   EnsemblBacteria; KPA88369; KPA88369; PF66_05141.
DR   PATRIC; fig|50340.43.peg.2850; -.
DR   Proteomes; UP000037931; 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:UP000037931};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KPA88369.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KPA88369.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KPA88369.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    132    150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    157    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    220    247       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    267    286       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    126       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      136    245       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   290 AA;  31994 MW;  9C6200A6BFCC939A CRC64;
     MPLPDFLASH PLAFVFCALI LGLIVGSFIN VVVWRLPKML ERDWRAQAHD VLGLPQAEPG
     TTYNLLLPHS HCPHCRHRIR AWENLPLLSY ALLRGKCSNC KAPISKRYPL TELACGLLSA
     FIAWHFGFGW PAGLLLVLTW GLLAMSLIDA DHQILPDALV LPLLWLGLIA NHFALFTSLS
     DALWGAVAGY LSLWSVYWLF KLLTGKEGMG HGDFKLLAML GAWGGWQILP LTILLSSLVG
     AVLGLMLLRL RNAQTSTPIP FGPYLAIAGW IALLWGGQIT TSYLHFAGFQ
//
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