(data stored in ACNUC7421 zone)

SWISSPROT: D4YYQ5_SPHJU

ID   D4YYQ5_SPHJU            Unreviewed;       150 AA.
AC   D4YYQ5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN   Name=ppiB {ECO:0000313|EMBL:BAI95487.1};
GN   OrderedLocusNames=SJA_C1-06530 {ECO:0000313|EMBL:BAI95487.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95487.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95487.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|RuleBase:RU363019}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000256|RuleBase:RU363019}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; AP010803; BAI95487.1; -; Genomic_DNA.
DR   RefSeq; WP_013039184.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06530; -.
DR   EnsemblBacteria; BAI95487; BAI95487; SJA_C1-06530.
DR   GeneID; 29272326; -.
DR   KEGG; sjp:SJA_C1-06530; -.
DR   eggNOG; ENOG4108R5K; Bacteria.
DR   eggNOG; COG0652; LUCA.
DR   HOGENOM; HOG000065981; -.
DR   KO; K01802; -.
DR   OMA; KAPHLDG; -.
DR   OrthoDB; POG091H01WZ; -.
DR   Proteomes; UP000007753; Chromosome 1.
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; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PTHR11071; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYQ5.
DR   SWISS-2DPAGE; D4YYQ5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:BAI95487.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN       14    150       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
SQ   SEQUENCE   150 AA;  16010 MW;  D19D020A5E3EF231 CRC64;
     MADDTLTLSL DSGGDVVIKL RPDLAPGHVE RITQLAKDGF YDGVVFHRVI PGFMAQGGDP
     TGTGMGGSKL PDLKAEFSRE PHVRGVCSMA RAMNPNSANS QFFICFDDAT FLDGQYTVWG
     EVTSGMEHVD ALPKGEPPKT PGKIVKATIS
//

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