ID   FKBA_AERHY              Reviewed;         268 AA.
AC   O08437;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-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;
DE   Flags: Precursor;
GN   Name=fkpA;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A6;
RX   PubMed=9171380; DOI=10.1128/jb.179.11.3397-3403.1997;
RA   Wong C.Y.F., Heuzenroeder M.W., Quinn D.M., Flower R.L.P.;
RT   "Cloning and characterization of two immunophilin-like genes, ilpA and
RT   fkpA, on a single 3.9-kilobase fragment of Aeromonas hydrophila genomic
RT   DNA.";
RL   J. Bacteriol. 179:3397-3403(1997).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. FkpA probably acts in the folding of extracytoplasmic
CC       proteins.
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; U56832; AAC45362.1; -; Genomic_DNA.
DR   RefSeq; WP_011704938.1; NZ_UFSL01000002.1.
DR   AlphaFoldDB; O08437; -.
DR   SMR; O08437; -.
DR   STRING; 1448139.AI20_14250; -.
DR   GeneID; 64357464; -.
DR   eggNOG; COG0545; Bacteria.
DR   OMA; KYMSGHI; -.
DR   OrthoDB; 1861282at2; -.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Isomerase; Periplasm; Rotamase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..268
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase FkpA"
FT                   /id="PRO_0000025539"
FT   DOMAIN          172..257
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   268 AA;  28686 MW;  5E88D74A830BE3FA CRC64;
     MNNFLKVSLL AAAVAVSLTA CQKDEKTAAN TAEVKAEASK PAEAPKAEAK SFEEQSGYAI
     GLSMGRYIAN TLERQQELGI KLDNSVILKG VTDGLGKEAK MTDEEIQKVL QQYDAKINEL
     TKAKADKDAV ENQKKGEEYL AANAKKEGVK STESGLQYQV EKMGTGAKPK ATDIVKVHYT
     GTLTDGTKFD SSVDRGEPAT FPLNQVIPGW TEGVQLMPVG SKFKFFLPSK LAYGEHGAGS
     IPANAVLVFD VELLAIEKPA ADGDNAKK