FKBP_NEIMB
ID FKBP_NEIMB Reviewed; 109 AA.
AC P0A0W2; P25138;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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; OrderedLocusNames=NMB0027;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=BNCV / Serogroup B;
RX PubMed=1371354; DOI=10.1073/pnas.89.4.1164;
RA Sampson B.A., Gotschlich E.C.;
RT "Neisseria meningitidis encodes an FK506-inhibitable rotamase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1164-1168(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: PPIases accelerate the folding of 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 -!- ACTIVITY REGULATION: Inhibited by FK506.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; M97859; AAA25455.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF40498.1; -; Genomic_DNA.
DR PIR; F81245; F81245.
DR RefSeq; NP_273093.1; NC_003112.2.
DR RefSeq; WP_002216146.1; NC_003112.2.
DR AlphaFoldDB; P0A0W2; -.
DR SMR; P0A0W2; -.
DR STRING; 122586.NMB0027; -.
DR PaxDb; P0A0W2; -.
DR EnsemblBacteria; AAF40498; AAF40498; NMB0027.
DR KEGG; nme:NMB0027; -.
DR PATRIC; fig|122586.8.peg.38; -.
DR HOGENOM; CLU_013615_12_0_4; -.
DR OMA; RVIAGWD; -.
DR Proteomes; UP000000425; Chromosome.
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 1: Evidence at protein level;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..109
FT /note="FK506-binding protein"
FT /id="PRO_0000075351"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT VARIANT 3
FT /note="G -> S (in strain: BNCV / Serogroup B)"
FT VARIANT 12
FT /note="G -> S (in strain: BNCV / Serogroup B)"
FT VARIANT 33
FT /note="N -> D (in strain: BNCV / Serogroup B)"
SQ SEQUENCE 109 AA; 11789 MW; F90A625F4899AE4B CRC64;
MGGLIIEDLQ EGFGKEAVKG KEITVHYTGW LENGTKFDSS LDRRQPLTIT LGVGQVIKGW
DEGFGGMKEG GKRKLTIPSE MGYGAHGAGG VIPPHATLIF EVELLKVYE
