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Database: UniProt
Entry: J0WR22_9CLOT
LinkDB: J0WR22_9CLOT
Original site: J0WR22_9CLOT 
ID   J0WR22_9CLOT            Unreviewed;       270 AA.
AC   J0WR22;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   10-APR-2019, entry version 28.
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=HMPREF1141_0271 {ECO:0000313|EMBL:EJF38866.1};
OS   Clostridium sp. MSTE9.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1105031 {ECO:0000313|EMBL:EJF38866.1, ECO:0000313|Proteomes:UP000004073};
RN   [1] {ECO:0000313|EMBL:EJF38866.1, ECO:0000313|Proteomes:UP000004073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSTE9 {ECO:0000313|EMBL:EJF38866.1,
RC   ECO:0000313|Proteomes:UP000004073};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Nelson K.E.;
RL   Submitted (MAY-2012) 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:EJF38866.1}.
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DR   EMBL; AKFU01000047; EJF38866.1; -; Genomic_DNA.
DR   STRING; 1105031.HMPREF1141_0271; -.
DR   MEROPS; A24.019; -.
DR   EnsemblBacteria; EJF38866; EJF38866; HMPREF1141_0271.
DR   PATRIC; fig|1105031.3.peg.2972; -.
DR   Proteomes; UP000004073; 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:UP000004073};
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:UP000004073};
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     12     37       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    127       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    136    157       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    163    185       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    197    226       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    246    266       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    102       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      113    225       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   270 AA;  29064 MW;  16B6B33ECAC14FC6 CRC64;
     MLLYELTPAL TAYLLFCTVV LGTVMGSFAA CTAWRIAVGE DFLRGRSHCD ECGHVLTAKE
     LVPVVSWLVQ RGKCRWCGAK ISVRCPVTEL LCAAAFMGIV LRYGITLQTL QYLILTVLLL
     TVALVDYDTG LIPNGLLLAI VIDWAVFTPF LNGGAFLQNV GSGLMSGLAA SVPLLLLTLL
     MDRTLRQESM GGGDIKFFFA AGLFFSIQGI LFLMLVSSVL GILFAALTKK TAGDPENPKA
     FPFGPAIAAG VYLSMLAAET AVEYYINLFL
//
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