ID   FKBX_ECOL6              Reviewed;         149 AA.
AC   P0AEM1; P22563;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   Name=fkpB; Synonyms=slpA; OrderedLocusNames=c0032;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. Substrate
CC       specificity carried out with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide',
CC       where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile >
CC       Lys = Ala > Trp > His >> Gln (By similarity). {ECO:0000250}.
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;
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN78532.1; -; Genomic_DNA.
DR   RefSeq; WP_000004655.1; NC_004431.1.
DR   AlphaFoldDB; P0AEM1; -.
DR   BMRB; P0AEM1; -.
DR   SMR; P0AEM1; -.
DR   STRING; 199310.c0032; -.
DR   EnsemblBacteria; AAN78532; AAN78532; c0032.
DR   GeneID; 67416103; -.
DR   KEGG; ecc:c0032; -.
DR   eggNOG; COG1047; Bacteria.
DR   HOGENOM; CLU_098197_3_0_6; -.
DR   OMA; FGQTEDH; -.
DR   BioCyc; ECOL199310:C0032-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Isomerase; Rotamase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..149
FT                   /note="FKBP-type 16 kDa peptidyl-prolyl cis-trans
FT                   isomerase"
FT                   /id="PRO_0000075371"
FT   DOMAIN          2..72
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   149 AA;  16081 MW;  485CB0472D571A6F CRC64;
     MSESVQSNSA VLVHFTLKLD DGTTAESTRN NGKPALFRLG DASLSEGLEQ HLLGLKVGDK
     TTFSLEPDAA FGVPSPDLIQ YFSRREFMDA GEPEIGAIML FTAMDGSEMP GVIREINGDS
     ITVDFNHPLA GQTVHFDIEV LEIDPALEA