PPIA_ECOL6
ID PPIA_ECOL6 Reviewed; 190 AA.
AC P0AFL4; P20752;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE Short=PPIase A;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin A;
DE AltName: Full=Rotamase A;
DE Flags: Precursor;
GN Name=ppiA; OrderedLocusNames=c4138;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN82576.1; -; Genomic_DNA.
DR RefSeq; WP_000477225.1; NC_004431.1.
DR AlphaFoldDB; P0AFL4; -.
DR BMRB; P0AFL4; -.
DR SMR; P0AFL4; -.
DR STRING; 199310.c4138; -.
DR EnsemblBacteria; AAN82576; AAN82576; c4138.
DR GeneID; 66672756; -.
DR KEGG; ecc:c4138; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_9_6; -.
DR OMA; VPFHRVM; -.
DR BioCyc; ECOL199310:C4138-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR PANTHER; PTHR43246; PTHR43246; 1.
DR Pfam; PF00160; Pro_isomerase; 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;
KW Isomerase; Periplasm; Rotamase; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..190
FT /note="Peptidyl-prolyl cis-trans isomerase A"
FT /id="PRO_0000045121"
FT DOMAIN 27..188
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 190 AA; 20431 MW; 8B48535F36AA61A2 CRC64;
MFKSTLAAMA AVFALSALSP AAMAAKGDPH VLLTTSAGNI ELELDKQKAP VSVQNFVDYV
NSGFYNNTTF HRVIPGFMIQ GGGFTEQMQQ KKPNPPIKNE ADNGLRNTRG TIAMARTADK
DSATSQFFIN VADNAFLDHG QRDFGYAVFG KVVKGMDVAD KISQVPTHDV GPYQNVPSKP
VVILSAKVLP
