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Database: UniProt
Entry: A0A0J5T1R3_9RHOB
LinkDB: A0A0J5T1R3_9RHOB
Original site: A0A0J5T1R3_9RHOB 
ID   A0A0J5T1R3_9RHOB        Unreviewed;       256 AA.
AC   A0A0J5T1R3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   16-JAN-2019, entry version 10.
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=IMCC21224_1660 {ECO:0000313|EMBL:KMK64002.1};
OS   Puniceibacterium sp. IMCC21224.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Puniceibacterium.
OX   NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK64002.1, ECO:0000313|Proteomes:UP000036046};
RN   [1] {ECO:0000313|EMBL:KMK64002.1, ECO:0000313|Proteomes:UP000036046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK64002.1,
RC   ECO:0000313|Proteomes:UP000036046};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21224 belonging to the
RT   Alphaproteobacteria.";
RL   Submitted (MAY-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:KMK64002.1}.
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DR   EMBL; LDPY01000006; KMK64002.1; -; Genomic_DNA.
DR   RefSeq; WP_047998326.1; NZ_LDPY01000006.1.
DR   EnsemblBacteria; KMK64002; KMK64002; IMCC21224_1660.
DR   PATRIC; fig|1618204.4.peg.5360; -.
DR   OrthoDB; 2046608at2; -.
DR   Proteomes; UP000036046; 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:UP000036046};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KMK64002.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KMK64002.1};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU003794};
KW   Protease {ECO:0000256|RuleBase:RU003794};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036046};
KW   Transferase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:KMK64002.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     99    118       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    125    142       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    200    221       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    233    253       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       14     92       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      107    212       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   256 AA;  26320 MW;  B26F3DD404C35CE6 CRC64;
     MSDTAVFAVL LLLLAPVMGS FLGVLIDRLP RGQNVVWPGS ACRSCHQRLG PCDLVPILSF
     ALSRGCCRHC GATIPPWLLY IEIATTGATG IAVILGQDMV AMAMIAALLW LLLGLGVADL
     LWFRLPDVMT GALLALALLW SLRVDGNPGG ALIGATLGAG SFAALRLGYR TLRGREGLGL
     GDVKLMAGLG ALLGPWDLPL LVLLAALAAL AATLGGALMS GRGRAALRAS RPLPFGAALA
     AAAAGLWLMR LSVVVG
//
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