(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NQ20_YERPA

ID   A0A0E1NQ20_YERPA        Unreviewed;       206 AA.
AC   A0A0E1NQ20;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   OrderedLocusNames=YPA_0082 {ECO:0000313|EMBL:ABG12051.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12051.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12051.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12051.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|RuleBase:RU003915}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000308; ABG12051.1; -; Genomic_DNA.
DR   RefSeq; WP_002228198.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12051; ABG12051; YPA_0082.
DR   EnsemblBacteria; AJJ79000; AJJ79000; CH58_2918.
DR   KEGG; ypa:YPA_0082; -.
DR   PATRIC; fig|360102.15.peg.3072; -.
DR   KO; K03773; -.
DR   OMA; THYHGTF; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.10.287.460; -; 1.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   InterPro; IPR036944; PPIase_FKBP_N_sf.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NQ20.
DR   SWISS-2DPAGE; A0A0E1NQ20.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915, ECO:0000313|EMBL:ABG12051.1};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915}.
SQ   SEQUENCE   206 AA;  22426 MW;  8D40A3EF76E39FCD CRC64;
     MTTPSFDSVE AQASYGIGLQ IGQQLQESGL QGLLPEALLA GLRDAMEGNT PTVPVDVIHR
     ALQEVHEKAD KVRIERQQAL VDEGKTFLEE NAKRDDVTTT ESGLQFSVLQ AGDGPIPSRQ
     DRVRVHYTGR LVDGTVFDSS VERGQPADFP VSGVIPGWIE ALSMMPVGSK WKLYIPHNLA
     YGERGAGATI PPFSALMFEV ELLEIL
//

If you have problems or comments...

PBIL Back to PBIL home page