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   02-SEP-2026, entry version 139.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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
RT   0-2.4 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}.
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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_CP009789.1.
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=73-144.
DR   AlphaFoldDB; P0AEM0; -.
DR   BMRB; P0AEM0; -.
DR   SMR; P0AEM0; -.
DR   BioGRID; 4262915; 208.
DR   DIP; DIP-35792N; -.
DR   FunCoup; P0AEM0; 91.
DR   IntAct; P0AEM0; 49.
DR   STRING; 511145.b0028; -.
DR   jPOST; P0AEM0; -.
DR   PaxDb; 511145-b0028; -.
DR   EnsemblBacteria; AAC73139; AAC73139; b0028.
DR   GeneID; 86944962; -.
DR   GeneID; 93777408; -.
DR   GeneID; 944807; -.
DR   KEGG; ecj:JW0026; -.
DR   KEGG; eco:b0028; -.
DR   KEGG; ecoc:C3026_00135; -.
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; AKFVMGD; -.
DR   OrthoDB; 9808891at2; -.
DR   PhylomeDB; P0AEM0; -.
DR   BioCyc; EcoCyc:EG11080-MONOMER; -.
DR   BioCyc; MetaCyc:EG11080-MONOMER; -.
DR   BRENDA; 5.2.1.8; 2026.
DR   EvolutionaryTrace; P0AEM0; -.
DR   PRO; PR:P0AEM0; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0AEM0; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   FunFam; 2.40.10.330:FF:000002; Peptidyl-prolyl cis-trans isomerase; 1.
DR   Gene3D; 2.40.10.330; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR048261; SlpA/SlyD-like_ins_sf.
DR   NCBIfam; NF011676; PRK15095.1; 1.
DR   PANTHER; PTHR47861:SF4; FKBP-TYPE 16 KDA PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR47861; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PDBsum; 2M2A; -.
DR   PDBsum; 4DT4; -.
DR   PDBsum; 5I7Q; -.
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"
FT   HELIX           145..148
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
//