FKBB_SHIFL
ID FKBB_SHIFL Reviewed; 206 AA.
AC P0A9L4; P39311; P76801; Q47717;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=FKBP-type 22 kDa peptidyl-prolyl cis-trans isomerase;
DE Short=FKBP22;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
GN Name=fklB; OrderedLocusNames=SF4279, S4544;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN45697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN45697.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_709990.3; NC_004337.2.
DR RefSeq; WP_000211225.1; NZ_WPGW01000133.1.
DR AlphaFoldDB; P0A9L4; -.
DR SMR; P0A9L4; -.
DR STRING; 198214.SF4279; -.
DR PRIDE; P0A9L4; -.
DR EnsemblBacteria; AAN45697; AAN45697; SF4279.
DR GeneID; 1023443; -.
DR GeneID; 66671873; -.
DR KEGG; sfl:SF4279; -.
DR PATRIC; fig|198214.7.peg.5048; -.
DR HOGENOM; CLU_013615_0_1_6; -.
DR OrthoDB; 1861282at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..206
FT /note="FKBP-type 22 kDa peptidyl-prolyl cis-trans
FT isomerase"
FT /id="PRO_0000075368"
FT DOMAIN 120..206
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 206 AA; 22216 MW; 5557F63673A101DE CRC64;
MTTPTFDTIE AQASYGIGLQ VGQQLSESGL EGLLPEALVA GIADALEGKH PAVPVDVVHR
ALREIHERAD AVRRQRFQAM AAEGVKYLEE NAKKEGVNST ESGLQFRVIN QGEGAIPART
DRVRVHYTGK LIDGTVFDSS VARGEPAEFP VNGVIPGWIE ALTLMPVGSK WELTIPQELA
YGERGAGASI PPFSTLVFEV ELLEIL
