ID   FKBA_ECOL6              Reviewed;         270 AA.
AC   P65764; Q8X880;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase FkpA;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=fkpA; OrderedLocusNames=c4121;
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. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82559.1; -; Genomic_DNA.
DR   RefSeq; WP_000838261.1; NC_004431.1.
DR   AlphaFoldDB; P65764; -.
DR   BMRB; P65764; -.
DR   SMR; P65764; -.
DR   STRING; 199310.c4121; -.
DR   EnsemblBacteria; AAN82559; AAN82559; c4121.
DR   GeneID; 66672773; -.
DR   KEGG; ecc:c4121; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_2_6; -.
DR   OMA; KYMSGHI; -.
DR   BioCyc; ECOL199310:C4121-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.10.287.460; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   InterPro; IPR036944; PPIase_FKBP_N_sf.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Periplasm; Rotamase; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..270
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase FkpA"
FT                   /id="PRO_0000025537"
FT   DOMAIN          164..249
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   270 AA;  28912 MW;  CEC73B8672AA72FE CRC64;
     MKSLFKVTLL ATTMAVALHA PITFAAEAAK PATTADSKAA FKNDDQKSAY ALGASLGRYM
     ENSLKEQEKL GIKLDKDQLI AGVQDAFADK SKLSDQEIEQ TLQAFEARVK SSAQAKMEKD
     AADNEAKGKE YREKFAKEKG VKTSSTGLVY QVVEAGKGEA PKDSDTVVVN YKGTLIDGKE
     FDNSYTRGEP LSFRLDGVIP GWTEGLKNIK KGGKIKLVIP PELAYGKAGV PGIPPNSTLV
     FDVELLDVKP APKADAKPEA DAKAADSAKK