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Database: UniProt
Entry: A0A1S1XB72_9NEIS
LinkDB: A0A1S1XB72_9NEIS
Original site: A0A1S1XB72_9NEIS 
ID   A0A1S1XB72_9NEIS        Unreviewed;       306 AA.
AC   A0A1S1XB72;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-FEB-2019, entry version 8.
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=BUE93_17395 {ECO:0000313|EMBL:PRP69545.1};
OS   Chromobacterium amazonense.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=1382803 {ECO:0000313|EMBL:PRP69545.1, ECO:0000313|Proteomes:UP000239469};
RN   [1] {ECO:0000313|EMBL:PRP69545.1, ECO:0000313|Proteomes:UP000239469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56AF {ECO:0000313|EMBL:PRP69545.1,
RC   ECO:0000313|Proteomes:UP000239469};
RA   Santos A.B., Nascimento A.M., Da Silva P.C.;
RT   "New insights into the genetic diversity of Chromobacterium isolated
RT   from tropical freshwater lake.";
RL   Submitted (JAN-2017) 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:PRP69545.1}.
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DR   EMBL; MTBD01000030; PRP69545.1; -; Genomic_DNA.
DR   RefSeq; WP_071109184.1; NZ_MTBD01000030.1.
DR   BioCyc; GCF_001855565:BI343_RS07055-MONOMER; -.
DR   Proteomes; UP000239469; 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:UP000239469};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|RuleBase:RU003794};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Transferase {ECO:0000256|RuleBase:RU003794};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794}.
SQ   SEQUENCE   306 AA;  32937 MW;  F5F0247999F535AC CRC64;
     MLQDMAWLLA THPAYLLGAA VVLGLMVGSF LNVVIHRMPR MLENEFLADS VGYLAESDRF
     PALKLAAQGA MEELTEAPGY NLWRPASHCP SCGAAVRAWQ NIPLLSYALL RGRCAACRVG
     ISPRYPLVES LCGVLFGFLA WKLGWGWPLF GAMALTAALL ALTFIDLDTQ LLPDSLTLPL
     MWAGLLFNLH GGLVPLSDAV LGAACGYLSL WLVYQLFKLA TGREGMGYGD FKLLAALGAW
     LGWSMLPLII LLSSLVGAVC GLAMMAASRV GRGQPIPFGP YLAAAGWIAL VWGPQIVEGY
     LAWLSR
//
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