ID   FKBP_NEIMC              Reviewed;         109 AA.
AC   P0A0W3; P25138;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=FK506-binding protein;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
GN   Name=fbp;
OS   Neisseria meningitidis serogroup C.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=135720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C114 / Serogroup C / Serotype 2b;
RX   PubMed=2895102; DOI=10.1128/jb.170.4.1691-1697.1988;
RA   Perry A.C.F., Nicolson I.J., Saunders J.R.;
RT   "Neisseria meningitidis C114 contains silent, truncated pilin genes that
RT   are homologous to Neisseria gonorrhoeae pil sequences.";
RL   J. Bacteriol. 170:1691-1697(1988).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M19305; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M19305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0A0W3; -.
DR   SMR; P0A0W3; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR044609; FKBP2/11.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR45779; PTHR45779; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Rotamase.
FT   CHAIN           1..109
FT                   /note="FK506-binding protein"
FT                   /id="PRO_0000075352"
FT   DOMAIN          20..108
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   109 AA;  11850 MW;  C0ADD3C249A39556 CRC64;
     MGSLIIEDLQ ESFGKEAVKG KEITVHYTGW LEDGTKFDSS LDRRQPLTIT LGVGQVIKGW
     DEGFGGMKEG GKRKLTIPSE MGYGAHGAGG VIPPHATLIF EVELLKVYE