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Database: UniProt
Entry: A0A135I3R5_9GAMM
LinkDB: A0A135I3R5_9GAMM
Original site: A0A135I3R5_9GAMM 
ID   A0A135I3R5_9GAMM        Unreviewed;       289 AA.
AC   A0A135I3R5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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=ATN88_13795 {ECO:0000313|EMBL:KXF80086.1};
OS   Enterovibrio coralii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Enterovibrio.
OX   NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF80086.1};
RN   [1] {ECO:0000313|EMBL:KXF80086.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF80086.1};
RA   Gomez-Gil B., Enciso-Ibarra J.;
RT   "Genomic Taxonomy of the Vibrionaceae.";
RL   Submitted (NOV-2015) 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:KXF80086.1}.
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DR   EMBL; LNTY01000058; KXF80086.1; -; Genomic_DNA.
DR   RefSeq; WP_067419728.1; NZ_LNTY01000058.1.
DR   EnsemblBacteria; KXF80086; KXF80086; ATN88_13795.
DR   BioCyc; GCF_001559595:ATN88_RS22190-MONOMER; -.
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   Hydrolase {ECO:0000256|RuleBase:RU003794};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KXF80086.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KXF80086.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     33       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    128    146       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    203       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    215    248       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    260    283       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       17    122       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      136    243       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   289 AA;  31975 MW;  F78A52BC34CBA6F5 CRC64;
     MNWLFDSLNL FVVFASVFGL IVGSFLNVVI YRLPKMMEIR WQQECHDCFP EEIAAPDGQV
     FNLSLPRSHC PNCQKQVNAI DNVPVLSWLI LGGKCRNCKT PVSKRYPLVE LLTAMLTGVT
     AFTLTGSYWS LAVIFATFVL IALCFIDIDT MLLPDQMTLP LMWAGMLLAV MGISPVSLQD
     SVIGAMAGYL SLWSVFQLFK LLTGKEGMGY GDFKLLAALG AWLGWQALPM VILLASFIGA
     VGGIIMIRIN GSDKETPFSF GPYLAIAGWI GLLWGDKIIN WYLTSYLGY
//
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