PPIA_ECOLI
ID PPIA_ECOLI Reviewed; 190 AA.
AC P0AFL3; P20752; Q2M729;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A {ECO:0000303|PubMed:2190212};
DE Short=PPIase A {ECO:0000303|PubMed:2190212};
DE EC=5.2.1.8 {ECO:0000269|PubMed:2190212};
DE AltName: Full=Cyclophilin A;
DE AltName: Full=Rotamase A {ECO:0000303|PubMed:2190212};
DE Flags: Precursor;
GN Name=ppiA; Synonyms=rot, rotA; OrderedLocusNames=b3363, JW3326;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2007139; DOI=10.1021/bi00226a009;
RA Hayano T., Takahashi N., Kato S., Maki N., Suzuki M.;
RT "Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed
RT separately in periplasmic and cytoplasmic compartments of Escherichia coli
RT cells.";
RL Biochemistry 30:3041-3048(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2546924; DOI=10.1128/jb.171.8.4525-4529.1989;
RA Kawamukai M., Matsuda H., Fujii W., Utsumi R., Komano T.;
RT "Nucleotide sequences of fic and fic-1 genes involved in cell filamentation
RT induced by cyclic AMP in Escherichia coli.";
RL J. Bacteriol. 171:4525-4529(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-190.
RX PubMed=2403545; DOI=10.1128/jb.172.1.397-410.1990;
RA Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.;
RT "Chromosomal organization and expression of Escherichia coli pabA.";
RL J. Bacteriol. 172:397-410(1990).
RN [6]
RP FUNCTION, PROTEIN SEQUENCE OF 25-36, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=2190212; DOI=10.1073/pnas.87.11.4028;
RA Liu J., Walsh C.T.;
RT "Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic
RT homolog of cyclophilin that is not inhibited by cyclosporin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4028-4032(1990).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=1606970; DOI=10.1111/j.1432-1033.1992.tb17002.x;
RA Compton L.A., Davis J.M., Macdonald J.R., Baechinger H.P.;
RT "Structural and functional characterization of Escherichia coli peptidyl-
RT prolyl cis-trans isomerases.";
RL Eur. J. Biochem. 206:927-934(1992).
RN [8]
RP MUTAGENESIS OF PHE-136.
RX PubMed=2001362; DOI=10.1021/bi00223a003;
RA Liu J., Chen C.-M., Walsh C.T.;
RT "Human and Escherichia coli cyclophilins: sensitivity to inhibition by the
RT immunosuppressant cyclosporin A correlates with a specific tryptophan
RT residue.";
RL Biochemistry 30:2306-2310(1991).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=8130188; DOI=10.1021/bi00176a004;
RA Clubb R.T., Ferguson S.B., Walsh C.T., Wagner G.;
RT "Three-dimensional solution structure of Escherichia coli periplasmic
RT cyclophilin.";
RL Biochemistry 33:2761-2772(1994).
RN [10]
RP STRUCTURE BY NMR OF MUTANT TRP-136.
RX PubMed=8180197; DOI=10.1021/bi00185a007;
RA Fejzo J., Etzkorn F.A., Clubb R.T., Shi Y., Walsh C.T., Wagner G.;
RT "The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in
RT nearly identical conformation as human cyclophilin.";
RL Biochemistry 33:5711-5720(1994).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (Probable). It
CC catalyzes the cis-trans isomerization of proline imidic peptide bonds
CC in oligopeptides (PubMed:2190212). {ECO:0000269|PubMed:2190212,
CC ECO:0000305}.
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; Evidence={ECO:0000269|PubMed:2190212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16238;
CC Evidence={ECO:0000269|PubMed:2190212};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16239;
CC Evidence={ECO:0000269|PubMed:2190212};
CC -!- ACTIVITY REGULATION: Inhibition by cyclosporin A with a Ki of 25 to 50
CC mu-mol, a concentration 1000-fold higher than that required for
CC eukaryotic PPIases. {ECO:0000269|PubMed:1606970}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2190212}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; M55429; AAA23451.1; -; Genomic_DNA.
DR EMBL; M28363; AAA23772.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58160.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76388.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77927.1; -; Genomic_DNA.
DR EMBL; M32354; AAA24261.1; -; Genomic_DNA.
DR PIR; A37964; CSECA.
DR RefSeq; NP_417822.1; NC_000913.3.
DR RefSeq; WP_000477225.1; NZ_STEB01000004.1.
DR PDB; 1CLH; NMR; -; A=25-190.
DR PDB; 1J2A; X-ray; 1.80 A; A=25-190.
DR PDB; 1V9T; X-ray; 1.70 A; A/B=25-190.
DR PDB; 1VAI; X-ray; 1.80 A; A/B=25-190.
DR PDBsum; 1CLH; -.
DR PDBsum; 1J2A; -.
DR PDBsum; 1V9T; -.
DR PDBsum; 1VAI; -.
DR AlphaFoldDB; P0AFL3; -.
DR BMRB; P0AFL3; -.
DR SMR; P0AFL3; -.
DR BioGRID; 4261085; 160.
DR DIP; DIP-48080N; -.
DR IntAct; P0AFL3; 1.
DR STRING; 511145.b3363; -.
DR DrugBank; DB08168; Coumarin 120.
DR SWISS-2DPAGE; P0AFL3; -.
DR jPOST; P0AFL3; -.
DR PaxDb; P0AFL3; -.
DR PRIDE; P0AFL3; -.
DR EnsemblBacteria; AAC76388; AAC76388; b3363.
DR EnsemblBacteria; BAE77927; BAE77927; BAE77927.
DR GeneID; 66672756; -.
DR GeneID; 947870; -.
DR KEGG; ecj:JW3326; -.
DR KEGG; eco:b3363; -.
DR PATRIC; fig|1411691.4.peg.3367; -.
DR EchoBASE; EB0750; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_9_6; -.
DR InParanoid; P0AFL3; -.
DR OMA; VPFHRVM; -.
DR PhylomeDB; P0AFL3; -.
DR BioCyc; EcoCyc:EG10757-MON; -.
DR BioCyc; MetaCyc:EG10757-MON; -.
DR EvolutionaryTrace; P0AFL3; -.
DR PRO; PR:P0AFL3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Periplasm;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2190212"
FT CHAIN 25..190
FT /note="Peptidyl-prolyl cis-trans isomerase A"
FT /id="PRO_0000025497"
FT DOMAIN 27..188
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MUTAGEN 136
FT /note="F->W: Enhances susceptibility to CSA inhibition."
FT /evidence="ECO:0000269|PubMed:2001362"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1V9T"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1V9T"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:1V9T"
FT TURN 62..67
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1V9T"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1V9T"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1CLH"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1V9T"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1V9T"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1V9T"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1V9T"
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
