ID   FKBA_BUCAP              Reviewed;         252 AA.
AC   Q8K943;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=BUsg_514;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM68057.1; -; Genomic_DNA.
DR   RefSeq; WP_011054023.1; NC_004061.1.
DR   AlphaFoldDB; Q8K943; -.
DR   SMR; Q8K943; -.
DR   STRING; 198804.BUsg_514; -.
DR   EnsemblBacteria; AAM68057; AAM68057; BUsg_514.
DR   KEGG; bas:BUsg_514; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_2_6; -.
DR   OMA; KYMSGHI; -.
DR   OrthoDB; 1861282at2; -.
DR   Proteomes; UP000000416; 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; Rotamase.
FT   CHAIN           1..252
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase FkpA"
FT                   /id="PRO_0000075365"
FT   DOMAIN          165..252
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   252 AA;  28737 MW;  BFAD9A3C5E33F9EC CRC64;
     MIVFLLKRIL LLYLIFFVPK SFSENLPFFK IKSYSEKKEF FQNDNEKVGY SLGVSLGNYV
     NESFERQKKM GINLDKYNIL LGVQDAISGN LKLSNEEIST ILQKLEKNLK NAAKIEFEKS
     EKENLIQGKL YMKKFSEMKG VSKTSSGLLY IIDKLGEGEE IKTKNAEITV HYKGSLINGT
     EFDSSYKRGK PITLMLKDVI LGWQEGLKYI KKGGKIKLII PPNLGYGSNR INEIPANSIL
     IFDIELLDIK NI