(data stored in SCRATCH zone)

SWISSPROT: A0LFR5_SYNFM

ID   A0LFR5_SYNFM            Unreviewed;       353 AA.
AC   A0LFR5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, 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=Sfum_0568 {ECO:0000313|EMBL:ABK16267.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16267.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16267.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK16267.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0568; -.
DR   EnsemblBacteria; ABK16267; ABK16267; Sfum_0568.
DR   KEGG; sfu:Sfum_0568; -.
DR   eggNOG; ENOG4108S1R; Bacteria.
DR   eggNOG; COG0760; LUCA.
DR   HOGENOM; HOG000014031; -.
DR   KO; K03769; -.
DR   OMA; KKEFAIN; -.
DR   Proteomes; UP000001784; 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   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   4: Predicted;
DR   PRODOM; A0LFR5.
DR   SWISS-2DPAGE; A0LFR5.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143328, ECO:0000313|EMBL:ABK16267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143327}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    353       Peptidylprolyl isomerase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007908831.
FT   DOMAIN      204    305       PpiC. {ECO:0000259|PROSITE:PS50198}.
FT   COILED      144    164       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   353 AA;  38831 MW;  320B74D50B3FCBD4 CRC64;
     MMRKGSRWIP AILASFFVVV FLSPVGAAEK AAKKDAKPTA ASNETAAKSG ASKEPAKGEK
     VAVVNGTVIT RAEYESETKR FERQMAMSGQ APDGAQVAEM KKKVLDGLVG REVLKQQAAK
     LGVKVDPAEV DKEIATLKQR FPNEDEFKKA LKNLNLTEES LKAQFTQDLG IRKMIDEQVA
     SKITITPEET KKFYDGNPEL FKTPEMVRAS HVLIKVDPKA GDADKAKAKE RITAAQKKVQ
     AGEDFAKVAK EVSECPSAAK GGDLDFFQRG QMVGPFEQAA FALKVGSVSD IVETQFGYHV
     IKVTDKKEAG VMKYDEIKDR IAQHLKQDRV NQQLAKYIEE LKAQAKIEIF PVN
//

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