P45523 (FKBA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Rotamase

Gene names

Name:	fkpA
Synonyms:	yzzS
Ordered Locus Names:	b3347, JW3309

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	270 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).
Subcellular location	Periplasm.
Sequence similarities	Belongs to the FKBP-type PPIase family. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein refolding Inferred from direct assay. Source: EcoliWiki
Cellular component	membrane Inferred from sequence or structural similarity. Source: RefGenome periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FK506 binding Inferred from sequence or structural similarity. Source: RefGenome peptidyl-prolyl cis-trans isomerase activity Inferred from sequence or structural similarity. Source: RefGenome protein binding Inferred from physical interaction. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.4

Chain

26 – 270

245

FKBP-type peptidyl-prolyl cis-trans isomerase fkpA

PRO_0000025536

Regions

Domain

164 – 249

86

PPIase FKBP-type

Secondary structure

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270

Helix Strand Turn

Details...

Helix

44 – 68

25

Turn

69 – 71

3

Helix

76 – 87

12

Helix

95 – 137

43

Beta strand

141 – 143

3

Beta strand

149 – 154

6

Beta strand

166 – 175

10

Beta strand

180 – 183

4

Helix

184 – 187

4

Beta strand

191 – 194

4

Helix

195 – 197

3

Helix

200 – 205

6

Helix

206 – 208

3

Beta strand

214 – 219

6

Helix

221 – 223

3

Turn

224 – 228

5

Beta strand

239 – 249

11

Sequences

	Sequence		Length	Mass (Da)
	P45523 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: DBC73B8676BB63EF	FASTA	270	28,882
	10 20 30 40 50 60 MKSLFKVTLL ATTMAVALHA PITFAAEAAK PATAADSKAA FKNDDQKSAY ALGASLGRYM 70 80 90 100 110 120 ENSLKEQEKL GIKLDKDQLI AGVQDAFADK SKLSDQEIEQ TLQAFEARVK SSAQAKMEKD 130 140 150 160 170 180 AADNEAKGKE YREKFAKEKG VKTSSTGLVY QVVEAGKGEA PKDSDTVVVN YKGTLIDGKE 190 200 210 220 230 240 FDNSYTRGEP LSFRLDGVIP GWTEGLKNIK KGGKIKLVIP PELAYGKAGV PGIPPNSTLV 250 260 270 FDVELLDVKP APKADAKPEA DAKAADSAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins." Horne S.M., Young K.D. Arch. Microbiol. 163:357-365(1995) [PubMed: 7540828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / CS109.
[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]	"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 26-37. Strain: K12 / EMG2.
[5]	"New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH." Missiakas D., Betton J.-M., Raina S. Mol. Microbiol. 21:871-884(1996) [PubMed: 8878048] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L28082 Genomic DNA. Translation: AAC41459.1.
U18997 Genomic DNA. Translation: AAA58144.1.
U00096 Genomic DNA. Translation: AAC76372.1.
AP009048 Genomic DNA. Translation: BAE77944.1.

PIR

I65035.

RefSeq

NP_417806.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q6H	X-ray	1.97	A/B	26-249	[»]
1Q6I	X-ray	2.25	A/B	26-249	[»]
1Q6U	X-ray	2.45	A	26-270	[»]

ProteinModelPortal

P45523.

SMR

P45523. Positions 40-249.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9625N.

IntAct

P45523. 16 interactions.

MINT

MINT-1228098.

2D gel databases

SWISS-2DPAGE

P45523.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001264; EBESCP00000001264; EBESCG00000001047.
EBESCT00000001265; EBESCP00000001265; EBESCG00000001047.
EBESCT00000015327; EBESCP00000014618; EBESCG00000014387.

GeneID

947850.

GenomeReviews

Gene locus JW3309 in contig AP009048_GR.
Gene locus b3347 in contig U00096_GR.

KEGG

ecj:JW3309.
eco:b3347.

PATRIC

32122126. VBIEscCol129921_3440.

Organism-specific databases

EchoBASE

EB2737.

EcoGene

EG12900. fkpA.

Phylogenomic databases

eggNOG

COG0545.

GeneTree

EBGT00050000010913.

HOGENOM

HBG731200.

OMA

AYGDRDT.

PhylomeDB

P45523.

ProtClustDB

PRK10902.

Enzyme and pathway databases

BioCyc

EcoCyc:G7716-MONOMER.

Gene expression databases

Genevestigator

P45523.

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

K03772.

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...

Other

DrugBank

DB00864. Tacrolimus.

Entry information

Entry name

FKBA_ECOLI

Accession

Primary (citable) accession number: P45523
Secondary accession number(s): P39175, Q2M712

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program