ID   FKBA_BUCBP              Reviewed;         251 AA.
AC   Q89A61;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase FkpA;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   Name=fkpA; OrderedLocusNames=bbp_476;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AE016826; AAO27182.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q89A61; -.
DR   SMR; Q89A61; -.
DR   STRING; 224915.bbp_476; -.
DR   EnsemblBacteria; AAO27182; AAO27182; bbp_476.
DR   KEGG; bab:bbp_476; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_2_6; -.
DR   OMA; KYMSGHI; -.
DR   Proteomes; UP000000601; Chromosome.
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; Reference proteome; Rotamase.
FT   CHAIN           1..251
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase FkpA"
FT                   /id="PRO_0000075366"
FT   DOMAIN          164..251
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   251 AA;  28358 MW;  B015A0B7B830E252 CRC64;
     MILLKIIHII FVMIFLSIFF PKSLYASTSL IRKDHIIQKN LENFDDQSAY ALGVSLGNYI
     NHSFREQKRL GVILDKNSLL SGIRDSLSGK TILSDQEISM ELIKLEKKLK YFEDIVLKKE
     AHNNKIQGDL YIKKMLKKKD ARHTSSGLVF FIKKKGSGKF LHDSDVITVH YKGSLINGNE
     FDNSYKRGQP LSFSLDSVIP GWIEGLKYIK KGGLIKLVIP PKLAYGETGV PGIPGNSTLI
     FEIELIDIQS K