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   27-MAR-2024, entry version 131.
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; Pseudomonadota; 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   PDB; 7ZFM; X-ray; 1.71 A; A/B=25-187.
DR   PDBsum; 1CLH; -.
DR   PDBsum; 1J2A; -.
DR   PDBsum; 1V9T; -.
DR   PDBsum; 1VAI; -.
DR   PDBsum; 7ZFM; -.
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   jPOST; P0AFL3; -.
DR   PaxDb; 511145-b3363; -.
DR   EnsemblBacteria; AAC76388; AAC76388; b3363.
DR   GeneID; 75206307; -.
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; SVWGQVI; -.
DR   OrthoDB; 9807797at2; -.
DR   PhylomeDB; P0AFL3; -.
DR   BioCyc; EcoCyc:EG10757-MONOMER; -.
DR   BioCyc; MetaCyc:EG10757-MONOMER; -.
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   CDD; cd01920; cyclophilin_EcCYP_like; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 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:SF12; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A; 1.
DR   PANTHER; PTHR43246; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   SWISS-2DPAGE; P0AFL3; -.
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
//