P0A9L3 (FKBB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FKBP-type 22 kDa peptidyl-prolyl cis-trans isomerase
Short name=FKBP22
Short name=PPIase
EC=5.2.1.8

Alternative name(s):
Rotamase

Gene names

Name:	fklB
Synonyms:	ytfC
Ordered Locus Names:	b4207, JW5746

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Strongly inhibited by FK506.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm. Periplasm. Note: According to Ref.1 it is periplasmic.
Sequence similarities	Belongs to the FKBP-type PPIase family. Contains 1 PPIase FKBP-type domain.
Mass spectrometry	Molecular mass is 22084±1.47 Da from positions 2 - 206. Determined by ESI. Ref.4
Sequence caution	The sequence AAA97103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Periplasm
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from Biological aspect of Ancestor. Source: RefGenome periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FK506 binding Inferred from Biological aspect of Ancestor. Source: RefGenome peptidyl-prolyl cis-trans isomerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	Chain	2 – 206	205	FKBP-type 22 kDa peptidyl-prolyl cis-trans isomerase		PRO_0000075367
Regions
	Domain	120 – 206	87	PPIase FKBP-type

Sequences

	Sequence		Length	Mass (Da)
	P0A9L3 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5557F63673A101DE	FASTA	206	22,216
	10 20 30 40 50 60 MTTPTFDTIE AQASYGIGLQ VGQQLSESGL EGLLPEALVA GIADALEGKH PAVPVDVVHR 70 80 90 100 110 120 ALREIHERAD AVRRQRFQAM AAEGVKYLEE NAKKEGVNST ESGLQFRVIN QGEGAIPART 130 140 150 160 170 180 DRVRVHYTGK LIDGTVFDSS VARGEPAEFP VNGVIPGWIE ALTLMPVGSK WELTIPQELA 190 200 YGERGAGASI PPFSTLVFEV ELLEIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Isolation and amino acid sequence of a new 22-kDa FKBP-like peptidyl-prolyl cis/trans-isomerase of Escherichia coli. Similarity to Mip-like proteins of pathogenic bacteria." Rahfeld J.-U., Ruecknagel P., Stoller G., Hornes S.M., Schierhorn A., Young K.D., Fischer G. J. Biol. Chem. 271:22130-22138(1996) [PubMed: 8703024] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-206, CHARACTERIZATION, MASS SPECTROMETRY.
[5]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / EMG2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14003 Genomic DNA. Translation: AAA97103.1. Different initiation. U00096 Genomic DNA. Translation: AAC77164.2. AP009048 Genomic DNA. Translation: BAE78208.1.
RefSeq	NP_418628.4. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A9L3.
SMR	P0A9L3. Positions 8-206.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31854N.
IntAct	P0A9L3. 7 interactions.
MINT	MINT-1238607.
2D gel databases
SWISS-2DPAGE	P0A9L3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004635; EBESCP00000004635; EBESCG00000003778. EBESCT00000017107; EBESCP00000016398; EBESCG00000016166.
GeneID	948726.
GenomeReviews	Gene locus JW5746 in contig AP009048_GR. Gene locus b4207 in contig U00096_GR.
KEGG	ecj:JW5746. eco:b4207.
PATRIC	32123989. VBIEscCol129921_4339.
Organism-specific databases
EchoBASE	EB2396.
EcoGene	EG12503. fklB.
Phylogenomic databases
eggNOG	COG0545.
GeneTree	EBGT00050000010913.
HOGENOM	HBG731200.
OMA	PYSALVF.
PhylomeDB	P0A9L3.
ProtClustDB	PRK11570.
Enzyme and pathway databases
BioCyc	EcoCyc:G7865-MONOMER. MetaCyc:G7865-MONOMER.
Gene expression databases
Genevestigator	P0A9L3.
Family and domain databases
InterPro	IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. IPR000774. PPIase_FKBP_N. [Graphical view]
Gene3D	G3DSA:1.10.287.460. PPIase_FKBP_N. 1 hit.
KO	K03773.
PANTHER	PTHR10516. PPIase_FKBP. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. PF01346. FKBP_N. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FKBB_ECOLI

Accession

Primary (citable) accession number: P0A9L3
Secondary accession number(s): P39311 , P76801, Q2M698, Q47717

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program