(data stored in SCRATCH zone)

SWISSPROT: Q5LWL7_RUEPO

ID   Q5LWL7_RUEPO            Unreviewed;       276 AA.
AC   Q5LWL7;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Peptidylprolyl isomerase {ECO:0000256|SAAS:SAAS00143148};
DE            EC=5.2.1.8 {ECO:0000256|SAAS:SAAS00143148};
GN   OrderedLocusNames=SPO0058 {ECO:0000313|EMBL:AAV93389.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93389.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93389.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93389.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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;
CC         Evidence={ECO:0000256|SAAS:SAAS01128631};
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DR   EMBL; CP000031; AAV93389.1; -; Genomic_DNA.
DR   STRING; 246200.SPO0058; -.
DR   EnsemblBacteria; AAV93389; AAV93389; SPO0058.
DR   KEGG; sil:SPO0058; -.
DR   eggNOG; ENOG4107TF3; Bacteria.
DR   eggNOG; COG0760; LUCA.
DR   HOGENOM; HOG000014031; -.
DR   KO; K03769; -.
DR   OMA; EEVHARH; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   4: Predicted;
DR   PRODOM; Q5LWL7.
DR   SWISS-2DPAGE; Q5LWL7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143328};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143327}.
FT   DOMAIN      128    217       PpiC. {ECO:0000259|PROSITE:PS50198}.
SQ   SEQUENCE   276 AA;  29715 MW;  13B32EF822C39440 CRC64;
     MPSLAFALVM ALPVAAETKA EADTVVARVN GEEITLGHMI IARASLPQQY QQLPDDVLFD
     GILDQLVQQT LLKQQQKGET PKQIVLSLEN EERSLLAGET IEEIMAVATT ETAIQAAYDA
     QYADGFGGEE YNASHILVPS EDEAKAVKEL LDNGADFAAT AKEKSTGPSG PNGGALGWFG
     AGAMVPEFEQ AVVALNAGQV SDPVQTQFGW HVIILNDKRK SEAPALDEVR DELAGRIQQD
     AIEARLAELT KDSEIEKPEL TGVEPAVLRQ LELVRE
//

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