ID   FKBY_HAEIN              Reviewed;         241 AA.
AC   P44760;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable FKBP-type peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   OrderedLocusNames=HI_0574;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (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; L42023; AAC22232.1; -; Genomic_DNA.
DR   PIR; A64155; A64155.
DR   RefSeq; NP_438731.1; NC_000907.1.
DR   RefSeq; WP_005694170.1; NC_000907.1.
DR   AlphaFoldDB; P44760; -.
DR   SMR; P44760; -.
DR   STRING; 71421.HI_0574; -.
DR   EnsemblBacteria; AAC22232; AAC22232; HI_0574.
DR   KEGG; hin:HI_0574; -.
DR   PATRIC; fig|71421.8.peg.594; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_2_6; -.
DR   OMA; KYMSGHI; -.
DR   PhylomeDB; P44760; -.
DR   BioCyc; HINF71421:G1GJ1-586-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..241
FT                   /note="Probable FKBP-type peptidyl-prolyl cis-trans
FT                   isomerase"
FT                   /id="PRO_0000075373"
FT   DOMAIN          150..241
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   241 AA;  26125 MW;  7AE029E4E747439F CRC64;
     MLKIQKLSIA ALMVSAVISG QVFAEDNTFD EKAASYAVGT LMGSQMKDLV DSHKEVIKYD
     NARILDGLKD ALEGKVDVRK DEKIQKTLES IEAKLVAASK AKAESIAKQA KEEGDKFRAE
     FAKGKDVKTT QSGLMYKIES AGKGDTIKST DTVKVHYTGK LPNGKVFDSS VERGQPVEFQ
     LDQVIKGWTE GLQLVKKGGK IQFVIAPELG YGEQGAGASI PPNSTLIFDV EVLDVNPKSE
     K