PPIC_ECOLI
ID PPIC_ECOLI Reviewed; 93 AA.
AC P0A9L5; P39159; Q2M884;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase C;
DE Short=PPIase C;
DE EC=5.2.1.8 {ECO:0000269|PubMed:8163020};
DE AltName: Full=Par10 {ECO:0000303|PubMed:15322281};
DE AltName: Full=Parvulin;
DE AltName: Full=Rotamase C;
GN Name=ppiC; Synonyms=parVA; OrderedLocusNames=b3775, JW3748;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-93.
RX PubMed=7925971; DOI=10.1016/0014-5793(94)00932-5;
RA Rahfeld J.-U., Ruecknagel K.P., Schelbert B., Ludwig B., Hacker J.,
RA Mann K., Fischer G.;
RT "Confirmation of the existence of a third family among peptidyl-prolyl
RT cis/trans isomerases. Amino acid sequence and recombinant production of
RT parvulin.";
RL FEBS Lett. 352:180-184(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 PROTEIN SEQUENCE OF 2-22, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=8163020; DOI=10.1016/0014-5793(94)80608-x;
RA Rahfeld J.-U., Schierhorn A., Mann K., Fischer G.;
RT "A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli.";
RL FEBS Lett. 343:65-69(1994).
RN [6]
RP IDENTIFICATION.
RX PubMed=7878732; DOI=10.1016/s0968-0004(00)88941-0;
RA Rudd K.E., Sofia H.J., Koonin E.V., Plunkett G. III, Lazar S.,
RA Rouviere P.E.;
RT "Conserved sequence motifs in bacterial and bacteriophage chaperonins.";
RL Trends Biochem. Sci. 20:14-15(1995).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=15322281; DOI=10.1110/ps.04756704;
RA Kuhlewein A., Voll G., Hernandez Alvarez B., Kessler H., Fischer G.,
RA Rahfeld J.-U., Gemmecker G.;
RT "Solution structure of Escherichia coli Par10: the prototypic member of the
RT parvulin family of peptidyl-prolyl cis/trans isomerases.";
RL Protein Sci. 13:2378-2387(2004).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (Probable). It
CC prefers amino acid residues with hydrophobic side chains like leucine
CC and phenylalanine in the P1 position of the peptides substrates.
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:8163020};
CC -!- ACTIVITY REGULATION: Not inhibited by cyclosporin A or FK506.
CC {ECO:0000269|PubMed:8163020}.
CC -!- INTERACTION:
CC P0A9L5; P37339: lhgD; NbExp=3; IntAct=EBI-555953, EBI-555990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000305}.
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DR EMBL; S73874; AAB32054.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67578.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76780.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77522.1; -; Genomic_DNA.
DR PIR; S48658; S48658.
DR RefSeq; NP_418223.1; NC_000913.3.
DR RefSeq; WP_001140251.1; NZ_STEB01000021.1.
DR PDB; 1JNS; NMR; -; A=2-93.
DR PDB; 1JNT; NMR; -; A=2-93.
DR PDBsum; 1JNS; -.
DR PDBsum; 1JNT; -.
DR AlphaFoldDB; P0A9L5; -.
DR BMRB; P0A9L5; -.
DR SMR; P0A9L5; -.
DR BioGRID; 4263314; 202.
DR BioGRID; 852585; 2.
DR DIP; DIP-48081N; -.
DR IntAct; P0A9L5; 13.
DR STRING; 511145.b3775; -.
DR jPOST; P0A9L5; -.
DR PaxDb; P0A9L5; -.
DR PRIDE; P0A9L5; -.
DR EnsemblBacteria; AAC76780; AAC76780; b3775.
DR EnsemblBacteria; BAE77522; BAE77522; BAE77522.
DR GeneID; 66672321; -.
DR GeneID; 948285; -.
DR KEGG; ecj:JW3748; -.
DR KEGG; eco:b3775; -.
DR PATRIC; fig|1411691.4.peg.2931; -.
DR EchoBASE; EB2256; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_090028_6_1_6; -.
DR InParanoid; P0A9L5; -.
DR OMA; GPVRTQF; -.
DR PhylomeDB; P0A9L5; -.
DR BioCyc; EcoCyc:EG12352-MON; -.
DR BioCyc; MetaCyc:EG12352-MON; -.
DR BRENDA; 5.2.1.8; 2026.
DR EvolutionaryTrace; P0A9L5; -.
DR PRO; PR:P0A9L5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isomerase;
KW Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7925971,
FT ECO:0000269|PubMed:8163020"
FT CHAIN 2..93
FT /note="Peptidyl-prolyl cis-trans isomerase C"
FT /id="PRO_0000193415"
FT DOMAIN 2..91
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:1JNS"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1JNS"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:1JNS"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:1JNS"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1JNS"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1JNS"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1JNT"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1JNS"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1JNT"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1JNS"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1JNS"
SQ SEQUENCE 93 AA; 10232 MW; 678A1BF2CBEA969B CRC64;
MAKTAAALHI LVKEEKLALD LLEQIKNGAD FGKLAKKHSI CPSGKRGGDL GEFRQGQMVP
AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRN
