FKBB_ECOLI
ID FKBB_ECOLI Reviewed; 206 AA.
AC P0A9L3; P39311; P76801; Q2M698; Q47717;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=FKBP-type 22 kDa peptidyl-prolyl cis-trans isomerase {ECO:0000303|PubMed:8703024};
DE Short=FKBP22;
DE Short=PPIase;
DE EC=5.2.1.8 {ECO:0000269|PubMed:8703024};
DE AltName: Full=Rotamase;
GN Name=fklB; Synonyms=ytfC; OrderedLocusNames=b4207, JW5746;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-206, MASS SPECTROMETRY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=8703024; DOI=10.1074/jbc.271.36.22130;
RA Rahfeld J.-U., Ruecknagel P., Stoller G., Hornes S.M., Schierhorn A.,
RA Young K.D., Fischer G.;
RT "Isolation and amino acid sequence of a new 22-kDa FKBP-like peptidyl-
RT prolyl cis/trans-isomerase of Escherichia coli. Similarity to Mip-like
RT proteins of pathogenic bacteria.";
RL J. Biol. Chem. 271:22130-22138(1996).
RN [5]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (Probable).
CC Catalyzes the cis-trans isomerization of proline imidic peptide bonds
CC in oligopeptides (PubMed:8703024). Displays a preference for substrates
CC with a lysyl residue in the P1 position (PubMed:8703024).
CC {ECO:0000269|PubMed:8703024, ECO:0000305}.
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: Strongly inhibited by FK506.
CC {ECO:0000269|PubMed:8703024}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8703024}.
CC -!- INTERACTION:
CC P0A9L3; P0A9L3: fklB; NbExp=3; IntAct=EBI-369295, EBI-369295;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Periplasm {ECO:0000269|PubMed:7610040,
CC ECO:0000269|PubMed:8703024}.
CC -!- MASS SPECTROMETRY: Mass=22084; Mass_error=1.47; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8703024};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97103.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97103.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77164.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78208.1; -; Genomic_DNA.
DR RefSeq; NP_418628.4; NC_000913.3.
DR RefSeq; WP_000211225.1; NZ_SSUV01000014.1.
DR AlphaFoldDB; P0A9L3; -.
DR SMR; P0A9L3; -.
DR BioGRID; 4259639; 18.
DR BioGRID; 853018; 5.
DR DIP; DIP-31854N; -.
DR IntAct; P0A9L3; 11.
DR MINT; P0A9L3; -.
DR STRING; 511145.b4207; -.
DR SWISS-2DPAGE; P0A9L3; -.
DR jPOST; P0A9L3; -.
DR PaxDb; P0A9L3; -.
DR PRIDE; P0A9L3; -.
DR EnsemblBacteria; AAC77164; AAC77164; b4207.
DR EnsemblBacteria; BAE78208; BAE78208; BAE78208.
DR GeneID; 66671873; -.
DR GeneID; 948726; -.
DR KEGG; ecj:JW5746; -.
DR KEGG; eco:b4207; -.
DR PATRIC; fig|1411691.4.peg.2494; -.
DR EchoBASE; EB2396; -.
DR eggNOG; COG0545; Bacteria.
DR HOGENOM; CLU_013615_0_3_6; -.
DR InParanoid; P0A9L3; -.
DR OMA; RVHYHGE; -.
DR PhylomeDB; P0A9L3; -.
DR BioCyc; EcoCyc:G7865-MON; -.
DR BioCyc; MetaCyc:G7865-MON; -.
DR BRENDA; 5.2.1.8; 2026.
DR PRO; PR:P0A9L3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005528; F:FK506 binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:EcoCyc.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IMP:EcoCyc.
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 Cytoplasm; Direct protein sequencing; Isomerase; Periplasm;
KW Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8703024,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..206
FT /note="FKBP-type 22 kDa peptidyl-prolyl cis-trans
FT isomerase"
FT /id="PRO_0000075367"
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
