PPI1_STAA8
ID PPI1_STAA8 Reviewed; 197 AA.
AC Q2FZU9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
GN OrderedLocusNames=SAOUHSC_00891;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD30016.1; -; Genomic_DNA.
DR RefSeq; WP_000035058.1; NZ_LS483365.1.
DR RefSeq; YP_499444.1; NC_007795.1.
DR AlphaFoldDB; Q2FZU9; -.
DR SMR; Q2FZU9; -.
DR STRING; 1280.SAXN108_0949; -.
DR EnsemblBacteria; ABD30016; ABD30016; SAOUHSC_00891.
DR GeneID; 3921737; -.
DR KEGG; sao:SAOUHSC_00891; -.
DR PATRIC; fig|93061.5.peg.811; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_0_9; -.
DR OMA; GEGYPGS; -.
DR PRO; PR:Q2FZU9; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..197
FT /note="Putative peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000299080"
FT DOMAIN 14..195
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 197 AA; 21619 MW; 71F2FE0713702B34 CRC64;
MANYPQLNKE VQQGEIKVVM HTNKGDMTFK LFPNIAPKTV ENFVTHAKNG YYDGITFHRV
INDFMIQGGD PTATGMGGES IYGGAFEDEF SLNAFNLYGA LSMANSGPNT NGSQFFIVQM
KEVPQNMLSQ LADGGWPQPI VDAYGEKGGT PWLDQKHTVF GQIIDGETTL EDIANTKVGP
QDKPLHDVVI ESIDVEE