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Database: UniProt
Entry: A0A222DY85_9RHOB
LinkDB: A0A222DY85_9RHOB
Original site: A0A222DY85_9RHOB 
ID   A0A222DY85_9RHOB        Unreviewed;       244 AA.
AC   A0A222DY85;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   13-FEB-2019, entry version 6.
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   Name=pppA {ECO:0000313|EMBL:ASP18934.1};
GN   ORFNames=ANTHELSMS3_00209 {ECO:0000313|EMBL:ASP18934.1};
OS   Antarctobacter heliothermus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Antarctobacter.
OX   NCBI_TaxID=74033 {ECO:0000313|EMBL:ASP18934.1, ECO:0000313|Proteomes:UP000203589};
RN   [1] {ECO:0000313|EMBL:ASP18934.1, ECO:0000313|Proteomes:UP000203589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS3 {ECO:0000313|EMBL:ASP18934.1,
RC   ECO:0000313|Proteomes:UP000203589};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA   Clarke A.K.;
RT   "Genome Sequence of Antarctobacter heliothermus Strain SMS3 Isolated
RT   from a culture of the Diatom Skeletonema marinoi.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP022540; ASP18934.1; -; Genomic_DNA.
DR   KEGG; aht:ANTHELSMS3_00209; -.
DR   KO; K02654; -.
DR   BioCyc; GCF_002237555:ANTHELSMS3_RS01055-MONOMER; -.
DR   Proteomes; UP000203589; Chromosome.
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:UP000203589};
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:UP000203589};
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     74     92       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    104    123       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    129    162       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    221    239       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       13     91       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      106    208       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   244 AA;  25713 MW;  42BDF95243A0C760 CRC64;
     MTALPTLLLL LLAPAIGSFL AVLVDRLPRG EDVVARPSHC RSCGARLGWR ELVPLLSYPI
     QRGRCRHCGT AFPGWLWLME VAALGLAVLA LLRGGSDWQV WCSAGLLWLL LALAVCDLIW
     FRLPDALTAA LAALCLGAAL AQGVFVQALA GGLLGMGSFL ALRLGYKALR RREGLGLGDV
     KLMAGLGALT GPFDLPLLVL VAAVGALCVT FALHRTLKGD LALPFGSALS GAGALLWLFE
     KTLL
//
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