(data stored in ACNUC7421 zone)

SWISSPROT: C8W312_DESAS

ID   C8W312_DESAS            Unreviewed;       327 AA.
AC   C8W312;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Peptidylprolyl isomerase {ECO:0000256|SAAS:SAAS00143148};
DE            EC=5.2.1.8 {ECO:0000256|SAAS:SAAS00143148};
GN   OrderedLocusNames=Dtox_0215 {ECO:0000313|EMBL:ACV61168.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61168.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61168.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV61168.1; -; Genomic_DNA.
DR   RefSeq; WP_015755889.1; NC_013216.1.
DR   STRING; 485916.Dtox_0215; -.
DR   EnsemblBacteria; ACV61168; ACV61168; Dtox_0215.
DR   KEGG; dae:Dtox_0215; -.
DR   eggNOG; ENOG4107UUG; Bacteria.
DR   eggNOG; COG0760; LUCA.
DR   HOGENOM; HOG000014031; -.
DR   KO; K03769; -.
DR   OMA; KKEFAIN; -.
DR   OrthoDB; 1838755at2; -.
DR   BioCyc; DACE485916:G1GFV-221-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8W312.
DR   SWISS-2DPAGE; C8W312.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143328, ECO:0000313|EMBL:ACV61168.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143327}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    327       Peptidylprolyl isomerase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007912172.
FT   DOMAIN      166    271       PpiC. {ECO:0000259|PROSITE:PS50198}.
SQ   SEQUENCE   327 AA;  37230 MW;  0EBD6DA76D5412AC CRC64;
     MRKIRISLFL LLGVLLLTGC NTNVVATVNG EEITQQQLDK RVSIVKDYYE KQYGQKIEGQ
     DAQKLIDNMK PGLLDEMISD TLKRQEARKV GKDMTDQQIQ EKIDGVKKQF PNEEAFKNFL
     AQQDLTEKDM AYMLNLQDVV LKDVKAPTEE EVQEYYDQNK EQFKTAEQYE VRHILISTDP
     DDAGNVKHTE AEAEKLAVQV LADIKNGKDF AALAREKSED LGSKDNGGLY TFKKGDTVPE
     FEKAALALKP GEYTREPVKT QFGYHIIKLE KLIPARDQSF AEVKDGIKQQ LDQEAKKNKF
     NAYLEDLKKK AKITNKLAET GDNKSKD
//

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