FKBX_SHIFL
ID FKBX_SHIFL Reviewed; 149 AA.
AC P0AEM3; P22563;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
GN Name=fkpB; Synonyms=slpA; OrderedLocusNames=SF0024, S0027;
GN and
GN Name=fkbP2; Synonyms=slpA; OrderedLocusNames=SF0025;
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. Substrate
CC specificity carried out with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide',
CC where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile >
CC Lys = Ala > Trp > His >> Gln (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; AE005674; AAN41690.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN41691.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15572.1; -; Genomic_DNA.
DR RefSeq; NP_705983.1; NC_004337.2.
DR RefSeq; NP_705984.1; NC_004337.2.
DR RefSeq; WP_000004655.1; NZ_WPGW01000005.1.
DR AlphaFoldDB; P0AEM3; -.
DR BMRB; P0AEM3; -.
DR SMR; P0AEM3; -.
DR STRING; 198214.SF0024; -.
DR EnsemblBacteria; AAN41690; AAN41690; SF0024.
DR EnsemblBacteria; AAN41691; AAN41691; SF0025.
DR EnsemblBacteria; AAP15572; AAP15572; S0027.
DR GeneID; 1024588; -.
DR GeneID; 1025951; -.
DR GeneID; 67416103; -.
DR KEGG; sfl:SF0024; -.
DR KEGG; sfl:SF0025; -.
DR KEGG; sfx:S0027; -.
DR PATRIC; fig|198214.7.peg.27; -.
DR HOGENOM; CLU_098197_3_0_6; -.
DR OMA; FGQTEDH; -.
DR OrthoDB; 2044224at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 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..149
FT /note="FKBP-type 16 kDa peptidyl-prolyl cis-trans
FT isomerase"
FT /id="PRO_0000075372"
FT DOMAIN 2..72
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 149 AA; 16081 MW; 485CB0472D571A6F CRC64;
MSESVQSNSA VLVHFTLKLD DGTTAESTRN NGKPALFRLG DASLSEGLEQ HLLGLKVGDK
TTFSLEPDAA FGVPSPDLIQ YFSRREFMDA GEPEIGAIML FTAMDGSEMP GVIREINGDS
ITVDFNHPLA GQTVHFDIEV LEIDPALEA