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Protein

FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase

Gene

fkpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

GO - Molecular functioni

  • FK506 binding Source: GO_Central
  • peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc

GO - Biological processi

  • chaperone-mediated protein folding Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciEcoCyc:EG11080-MONOMER.
ECOL316407:JW0026-MONOMER.
MetaCyc:EG11080-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Rotamase
Gene namesi
Name:fkpB
Synonyms:slpA, yaaD
Ordered Locus Names:b0028, JW0026
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11080. fkpB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 149148FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerasePRO_0000075369Add
BLAST

Proteomic databases

EPDiP0AEM0.
PaxDbiP0AEM0.
PRIDEiP0AEM0.

Interactioni

Protein-protein interaction databases

BioGridi4262915. 177 interactions.
DIPiDIP-35792N.
IntActiP0AEM0. 30 interactions.
STRINGi511145.b0028.

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 1910Combined sources
Beta strandi24 – 274Combined sources
Helixi28 – 314Combined sources
Beta strandi35 – 384Combined sources
Beta strandi41 – 444Combined sources
Helixi46 – 527Combined sources
Beta strandi60 – 656Combined sources
Helixi67 – 693Combined sources
Helixi76 – 783Combined sources
Beta strandi79 – 835Combined sources
Helixi84 – 874Combined sources
Turni88 – 903Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi108 – 11710Combined sources
Beta strandi120 – 1245Combined sources
Turni128 – 1314Combined sources
Beta strandi134 – 14411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M2ANMR-A1-148[»]
4DT4X-ray1.35A1-149[»]
ProteinModelPortaliP0AEM0.
SMRiP0AEM0. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7271PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG41090X3. Bacteria.
COG1047. LUCA.
HOGENOMiHOG000154890.
InParanoidiP0AEM0.
KOiK03774.
OMAiTLHFALR.
OrthoDBiEOG6Q8J79.
PhylomeDBiP0AEM0.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESVQSNSA VLVHFTLKLD DGTTAESTRN NGKPALFRLG DASLSEGLEQ
60 70 80 90 100
HLLGLKVGDK TTFSLEPDAA FGVPSPDLIQ YFSRREFMDA GEPEIGAIML
110 120 130 140
FTAMDGSEMP GVIREINGDS ITVDFNHPLA GQTVHFDIEV LEIDPALEA
Length:149
Mass (Da):16,081
Last modified:January 23, 2007 - v2
Checksum:i485CB0472D571A6F
GO

Mass spectrometryi

Molecular mass is 15946 Da from positions 2 - 149. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54945 Genomic DNA. Translation: CAA38706.1.
U00096 Genomic DNA. Translation: AAC73139.1.
AP009048 Genomic DNA. Translation: BAB96597.1.
PIRiJE0402.
RefSeqiNP_414569.1. NC_000913.3.
WP_000004655.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73139; AAC73139; b0028.
BAB96597; BAB96597; BAB96597.
GeneIDi944807.
KEGGiecj:JW0026.
eco:b0028.
PATRICi32115147. VBIEscCol129921_0025.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54945 Genomic DNA. Translation: CAA38706.1.
U00096 Genomic DNA. Translation: AAC73139.1.
AP009048 Genomic DNA. Translation: BAB96597.1.
PIRiJE0402.
RefSeqiNP_414569.1. NC_000913.3.
WP_000004655.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M2ANMR-A1-148[»]
4DT4X-ray1.35A1-149[»]
ProteinModelPortaliP0AEM0.
SMRiP0AEM0. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262915. 177 interactions.
DIPiDIP-35792N.
IntActiP0AEM0. 30 interactions.
STRINGi511145.b0028.

Proteomic databases

EPDiP0AEM0.
PaxDbiP0AEM0.
PRIDEiP0AEM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73139; AAC73139; b0028.
BAB96597; BAB96597; BAB96597.
GeneIDi944807.
KEGGiecj:JW0026.
eco:b0028.
PATRICi32115147. VBIEscCol129921_0025.

Organism-specific databases

EchoBASEiEB1072.
EcoGeneiEG11080. fkpB.

Phylogenomic databases

eggNOGiENOG41090X3. Bacteria.
COG1047. LUCA.
HOGENOMiHOG000154890.
InParanoidiP0AEM0.
KOiK03774.
OMAiTLHFALR.
OrthoDBiEOG6Q8J79.
PhylomeDBiP0AEM0.

Enzyme and pathway databases

BioCyciEcoCyc:EG11080-MONOMER.
ECOL316407:JW0026-MONOMER.
MetaCyc:EG11080-MONOMER.

Miscellaneous databases

PROiP0AEM0.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the lsp-dapB interval in Escherichia coli."
    Bouvier J., Stragier P.
    Nucleic Acids Res. 19:180-180(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase."
    Hottenrott S., Schumann T., Plueckthun A., Fischer G., Rahfeld J.-U.
    J. Biol. Chem. 272:15697-15701(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
    Strain: BL21.

Entry informationi

Entry nameiFKBX_ECOLI
AccessioniPrimary (citable) accession number: P0AEM0
Secondary accession number(s): P22563
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.