FKBX_ECOLI
ID FKBX_ECOLI Reviewed; 149 AA.
AC P0AEM0; P22563;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase {ECO:0000303|PubMed:9188461};
DE EC=5.2.1.8 {ECO:0000269|PubMed:9188461};
DE AltName: Full=Rotamase;
GN Name=fkpB; Synonyms=slpA, yaaD; OrderedLocusNames=b0028, JW0026;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2011499; DOI=10.1093/nar/19.1.180;
RA Bouvier J., Stragier P.;
RT "Nucleotide sequence of the lsp-dapB interval in Escherichia coli.";
RL Nucleic Acids Res. 19:180-180(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 MASS SPECTROMETRY, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=BL21;
RX PubMed=9188461; DOI=10.1074/jbc.272.25.15697;
RA Hottenrott S., Schumann T., Plueckthun A., Fischer G., Rahfeld J.-U.;
RT "The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl
RT cis/trans-isomerase.";
RL J. Biol. Chem. 272:15697-15701(1997).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (Probable).
CC Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-
CC nitroanilide' where Xaa is the amino acid tested, was found to be Phe >
CC Leu >> Ile > Lys = Ala > Trp > His >> Gln (PubMed:9188461).
CC {ECO:0000269|PubMed:9188461, 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:9188461};
CC -!- ACTIVITY REGULATION: Reversibly inhibited by Ni(2+) ions.
CC {ECO:0000269|PubMed:9188461}.
CC -!- MASS SPECTROMETRY: Mass=15946; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9188461};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54945; CAA38706.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73139.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96597.1; -; Genomic_DNA.
DR PIR; JE0402; JE0402.
DR RefSeq; NP_414569.1; NC_000913.3.
DR RefSeq; WP_000004655.1; NZ_STEB01000010.1.
DR PDB; 2M2A; NMR; -; A=1-148.
DR PDB; 4DT4; X-ray; 1.35 A; A=1-149.
DR PDB; 5I7Q; X-ray; 1.90 A; A=73-132.
DR PDBsum; 2M2A; -.
DR PDBsum; 4DT4; -.
DR PDBsum; 5I7Q; -.
DR AlphaFoldDB; P0AEM0; -.
DR BMRB; P0AEM0; -.
DR SMR; P0AEM0; -.
DR BioGRID; 4262915; 177.
DR DIP; DIP-35792N; -.
DR IntAct; P0AEM0; 49.
DR STRING; 511145.b0028; -.
DR jPOST; P0AEM0; -.
DR PaxDb; P0AEM0; -.
DR PRIDE; P0AEM0; -.
DR EnsemblBacteria; AAC73139; AAC73139; b0028.
DR EnsemblBacteria; BAB96597; BAB96597; BAB96597.
DR GeneID; 67416103; -.
DR GeneID; 944807; -.
DR KEGG; ecj:JW0026; -.
DR KEGG; eco:b0028; -.
DR PATRIC; fig|1411691.4.peg.2257; -.
DR EchoBASE; EB1072; -.
DR eggNOG; COG1047; Bacteria.
DR HOGENOM; CLU_098197_3_0_6; -.
DR InParanoid; P0AEM0; -.
DR OMA; FGQTEDH; -.
DR PhylomeDB; P0AEM0; -.
DR BioCyc; EcoCyc:EG11080-MON; -.
DR BioCyc; MetaCyc:EG11080-MON; -.
DR PRO; PR:P0AEM0; -.
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:0042026; P:protein refolding; IBA:GO_Central.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..149
FT /note="FKBP-type 16 kDa peptidyl-prolyl cis-trans
FT isomerase"
FT /id="PRO_0000075369"
FT DOMAIN 2..72
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT STRAND 10..19
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4DT4"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4DT4"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4DT4"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4DT4"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4DT4"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:4DT4"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4DT4"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:4DT4"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:4DT4"
SQ SEQUENCE 149 AA; 16081 MW; 485CB0472D571A6F CRC64;
MSESVQSNSA VLVHFTLKLD DGTTAESTRN NGKPALFRLG DASLSEGLEQ HLLGLKVGDK
TTFSLEPDAA FGVPSPDLIQ YFSRREFMDA GEPEIGAIML FTAMDGSEMP GVIREINGDS
ITVDFNHPLA GQTVHFDIEV LEIDPALEA
