(data stored in ACNUC1104 zone)

SWISSPROT: A4F5R3_SACEN

ID   A4F5R3_SACEN            Unreviewed;       172 AA.
AC   A4F5R3;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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   OrderedLocusNames=SACE_0034 {ECO:0000313|EMBL:CAL99387.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99387.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99387.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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:
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|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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; AM420293; CAL99387.1; -; Genomic_DNA.
DR   RefSeq; WP_009945653.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0034; -.
DR   EnsemblBacteria; CAL99387; CAL99387; SACE_0034.
DR   KEGG; sen:SACE_0034; -.
DR   eggNOG; ENOG4107XH4; Bacteria.
DR   eggNOG; COG0652; LUCA.
DR   HOGENOM; HOG000065981; -.
DR   KO; K03767; -.
DR   OMA; TSIYGQK; -.
DR   OrthoDB; 1861282at2; -.
DR   BioCyc; SERY405948:SACE_RS00165-MONOMER; -.
DR   Proteomes; UP000006728; 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; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
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; A4F5R3.
DR   SWISS-2DPAGE; A4F5R3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
KW   Isomerase {ECO:0000256|RuleBase:RU363019,
KW   ECO:0000313|EMBL:CAL99387.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN        1    167       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
SQ   SEQUENCE   172 AA;  18482 MW;  53AD417F85BF16E6 CRC64;
     MTATLHTTQG DIRVNLFPNK APKTVANFVG LAEGTKEYDA PNAKGERSGP FYDGVIFHRV
     IEGFMIQTGD PTGTGRGGPG YQFGDEFHPE LQFDRPYLLA MANAGPGTNG SQFFITVGAT
     SWLNYKHTIF GEVSDQASRD VVDAIATTAT GPADRPVNDI VIEKVTVERG EG
//

If you have problems or comments...

PBIL Back to PBIL home page