PPIB_ECOLI
ID PPIB_ECOLI Reviewed; 164 AA.
AC P23869; P78052; Q2MBQ4;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE Short=PPIase B;
DE EC=5.2.1.8 {ECO:0000269|PubMed:1606970, ECO:0000269|PubMed:2007139};
DE AltName: Full=Rotamase B;
GN Name=ppiB; OrderedLocusNames=b0525, JW0514;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
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 [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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RC STRAIN=K12;
RX PubMed=1864365; DOI=10.1016/0014-5793(91)80968-9;
RA Avalos J., Corrochano L.M., Brenner S.;
RT "Cysteinyl-tRNA synthetase is a direct descendant of the first aminoacyl-
RT tRNA synthetase.";
RL FEBS Lett. 286:176-180(1991).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY
RP 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 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8601841; DOI=10.1006/jmbi.1996.0136;
RA Konno M., Ito M., Hayano T., Takahashi N.;
RT "The substrate-binding site in Escherichia coli cyclophilin A preferably
RT recognizes a cis-proline isomer or a highly distorted form of the trans
RT isomer.";
RL J. Mol. Biol. 256:897-908(1996).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000269|PubMed:1606970,
CC ECO:0000269|PubMed:2007139}.
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:1606970,
CC ECO:0000269|PubMed:2007139};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16238;
CC Evidence={ECO:0000269|PubMed:1606970, ECO:0000269|PubMed:2007139};
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 -!- INTERACTION:
CC P23869; P16918: rhsC; NbExp=6; IntAct=EBI-555935, EBI-546818;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1606970,
CC ECO:0000269|PubMed:2007139}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; M55430; AAA23453.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73627.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76302.1; -; Genomic_DNA.
DR EMBL; X59293; CAA41982.1; -; Genomic_DNA.
DR PIR; D64784; CSECB.
DR RefSeq; NP_415058.1; NC_000913.3.
DR RefSeq; WP_000255997.1; NZ_STEB01000007.1.
DR PDB; 1LOP; X-ray; 1.80 A; A=1-164.
DR PDB; 2NUL; X-ray; 2.10 A; A=1-164.
DR PDB; 2RS4; NMR; -; A=1-164.
DR PDB; 7N3J; X-ray; 2.00 A; A/B=1-164.
DR PDBsum; 1LOP; -.
DR PDBsum; 2NUL; -.
DR PDBsum; 2RS4; -.
DR PDBsum; 7N3J; -.
DR AlphaFoldDB; P23869; -.
DR BMRB; P23869; -.
DR SMR; P23869; -.
DR BioGRID; 4262014; 40.
DR BioGRID; 853282; 1.
DR DIP; DIP-10546N; -.
DR IntAct; P23869; 23.
DR STRING; 511145.b0525; -.
DR SWISS-2DPAGE; P23869; -.
DR jPOST; P23869; -.
DR PaxDb; P23869; -.
DR PRIDE; P23869; -.
DR EnsemblBacteria; AAC73627; AAC73627; b0525.
DR EnsemblBacteria; BAE76302; BAE76302; BAE76302.
DR GeneID; 949038; -.
DR KEGG; ecj:JW0514; -.
DR KEGG; eco:b0525; -.
DR PATRIC; fig|1411691.4.peg.1753; -.
DR EchoBASE; EB0751; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_9_6; -.
DR InParanoid; P23869; -.
DR OMA; ELYNDHA; -.
DR PhylomeDB; P23869; -.
DR BioCyc; EcoCyc:EG10758-MON; -.
DR BioCyc; MetaCyc:EG10758-MON; -.
DR EvolutionaryTrace; P23869; -.
DR PRO; PR:P23869; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IMP:EcoCyc.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
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 PIRSF; PIRSF001467; Peptidylpro_ismrse; 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; Cytoplasm; Direct protein sequencing; Isomerase;
KW Reference proteome; Rotamase.
FT CHAIN 1..164
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000064202"
FT DOMAIN 1..162
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CONFLICT 132
FT /note="V -> E (in Ref. 1; AAA23453)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:1LOP"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1LOP"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1LOP"
FT TURN 33..38
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1LOP"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1LOP"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1LOP"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:7N3J"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2RS4"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2NUL"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1LOP"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1LOP"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1LOP"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1LOP"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1LOP"
SQ SEQUENCE 164 AA; 18153 MW; 4D5C7D2D8B02C810 CRC64;
MVTFHTNHGD IVIKTFDDKA PETVKNFLDY CREGFYNNTI FHRVINGFMI QGGGFEPGMK
QKATKEPIKN EANNGLKNTR GTLAMARTQA PHSATAQFFI NVVDNDFLNF SGESLQGWGY
CVFAEVVDGM DVVDKIKGVA TGRSGMHQDV PKEDVIIESV TVSE
