(data stored in SCRATCH zone)

SWISSPROT: A0A0H2Y392_YERPA

ID   A0A0H2Y392_YERPA        Unreviewed;       280 AA.
AC   A0A0H2Y392;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 13.
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   OrderedLocusNames=YPA_0463 {ECO:0000313|EMBL:ABG12431.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12431.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12431.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12431.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12431.1; -; Genomic_DNA.
DR   RefSeq; WP_002214096.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12431; ABG12431; YPA_0463.
DR   KEGG; ypa:YPA_0463; -.
DR   KO; K02464; -.
DR   OMA; RGKCAFC; -.
DR   BioCyc; YPES360102:GHZU-484-MONOMER; -.
DR   Proteomes; UP000001971; 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;
DR   PRODOM; A0A0H2Y392.
DR   SWISS-2DPAGE; A0A0H2Y392.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Hydrolase {ECO:0000256|RuleBase:RU003794,
KW   ECO:0000313|EMBL:ABG12431.1}; 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   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      6     29       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    119       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    168    193       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    213    240       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    252    271       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       13    118       DiS_P_DiS. {ECO:0000259|Pfam:PF06750}.
FT   DOMAIN      129    236       Peptidase_A24. {ECO:0000259|Pfam:
FT                                PF01478}.
SQ   SEQUENCE   280 AA;  31662 MW;  3ADA3F9C9EC537AB CRC64;
     MMDIQVFFVS YLIFGAMVGS FLNVLIYRLP IMLANLSSRS ESHGEEIKMR SHLRNINLFQ
     PGSFCHHCNE SIPIKYNIPI LGWIFLRGAS RCCNKKISTR YLFIEVLAVI QTLLVLMIFK
     EDLLICTSLV LIWSLTALAF IDFDTYLLPD CMTIPLLWLG LLINIDTVFA PLTSAVLGAV
     SGYLFLWLSY WLFKIVRGVD GMGYGDFKLM AALGAWFGVS AVPFLILFSS FFGLVAYAIF
     YFFDKKDNGK EINYIAFGPY ISLAGVLYLF LGSHVTNLFS
//

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