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Database: UniProt
Entry: A0A099CU31_9GAMM
LinkDB: A0A099CU31_9GAMM
Original site: A0A099CU31_9GAMM 
ID   A0A099CU31_9GAMM        Unreviewed;       283 AA.
AC   A0A099CU31;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   05-DEC-2018, entry version 18.
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=LF63_0111735 {ECO:0000313|EMBL:KGI77299.1};
OS   Oleiagrimonas soli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Oleiagrimonas.
OX   NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI77299.1, ECO:0000313|Proteomes:UP000029708};
RN   [1] {ECO:0000313|EMBL:KGI77299.1, ECO:0000313|Proteomes:UP000029708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3.5X {ECO:0000313|EMBL:KGI77299.1,
RC   ECO:0000313|Proteomes:UP000029708};
RA   Fang T., Wang H.;
RT   "Xanthomonadaceae 3.5X direct submission.";
RL   Submitted (SEP-2014) 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:KGI77299.1}.
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DR   EMBL; JROI01000013; KGI77299.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGI77299; KGI77299; LF63_0111735.
DR   Proteomes; UP000029708; 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:UP000029708};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KGI77299.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029708};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KGI77299.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     29       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     99    117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    123    141       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    153    170       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    176    197       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    209    242       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    262    282       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       13    119       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      129    238       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   283 AA;  31578 MW;  7A891F1872FBCD1A CRC64;
     MLPYWAWIVV AGVLGLMVGS FLNVVMLRLP ERMAFAWRNE AREILELEAV DETAPPDLVR
     QPSHCPQCKH RLSARDNIPL FGWLLLGGRC RYCKARISIQ YPLVELLTAL LSAAIVWRFG
     PGWVGLAGLV FTWILVAASG IDFRTQLLPD QLTYPLLWLG LLLSLLPMFV LPHTAILAAA
     IGYLSLWSLY WLFKLLTGKE GMGYGDFKLL AALGAWMGPM ALLPIMLLSS LIGAIVGVSL
     IALRKHERDV PMPFGPFIAA AGWTWFVFGP WLMHAYAVFF GLR
//
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