P0A9L5 (PPIC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase C
Short name=PPIase C
EC=5.2.1.8

Alternative name(s):
Par10
Parvulin
Rotamase C

Gene names

Name:	ppiC
Synonyms:	parVA
Ordered Locus Names:	b3775, JW3748

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	93 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 prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the ppiC/parvulin rotamase family. Contains 1 PpiC domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.5

Chain

2 – 93

92

Peptidyl-prolyl cis-trans isomerase C

PRO_0000193415

Regions

Domain

2 – 91

90

PpiC

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

93

Helix Strand Turn

Details...

Beta strand

4 – 14

11

Helix

15 – 27

13

Helix

31 – 39

9

Turn

42 – 46

5

Helix

47 – 49

3

Beta strand

52 – 54

3

Helix

60 – 68

9

Beta strand

75 – 80

6

Beta strand

83 – 90

8

Sequences

	Sequence		Length	Mass (Da)
	P0A9L5 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 678A1BF2CBEA969B	FASTA	93	10,232
	10 20 30 40 50 60 MAKTAAALHI LVKEEKLALD LLEQIKNGAD FGKLAKKHSI CPSGKRGGDL GEFRQGQMVP 70 80 90 AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin." Rahfeld J.-U., Ruecknagel K.P., Schelbert B., Ludwig B., Hacker J., Mann K., Fischer G. FEBS Lett. 352:180-184(1994) [PubMed: 7925971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-93.
[2]	"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed: 1379743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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], SEQUENCE REVISION. 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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli." Rahfeld J.-U., Schierhorn A., Mann K., Fischer G. FEBS Lett. 343:65-69(1994) [PubMed: 8163020] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22, CHARACTERIZATION.
[6]	"Conserved sequence motifs in bacterial and bacteriophage chaperonins." Rudd K.E., Sofia H.J., Koonin E.V., Plunkett G. III, Lazar S., Rouviere P.E. Trends Biochem. Sci. 20:14-15(1995) [PubMed: 7878732] [Abstract] Cited for: IDENTIFICATION.
[7]	"Solution structure of Escherichia coli Par10: the prototypic member of the parvulin family of peptidyl-prolyl cis/trans isomerases." Kuhlewein A., Voll G., Hernandez Alvarez B., Kessler H., Fischer G., Rahfeld J.-U., Gemmecker G. Protein Sci. 13:2378-2387(2004) [PubMed: 15322281] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S73874 Genomic DNA. Translation: AAB32054.1.
M87049 Genomic DNA. Translation: AAA67578.1.
U00096 Genomic DNA. Translation: AAC76780.1.
AP009048 Genomic DNA. Translation: BAE77522.1.

PIR

S48658.

RefSeq

NP_418223.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JNS	NMR	-	A	2-93	[»]
1JNT	NMR	-	A	2-93	[»]

ProteinModelPortal

P0A9L5.

SMR

P0A9L5. Positions 2-93.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48081N.

IntAct

P0A9L5. 13 interactions.

MINT

MINT-1225694.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003887; EBESCP00000003887; EBESCG00000003179.
EBESCT00000018396; EBESCP00000017687; EBESCG00000017450.

GeneID

948285.

GenomeReviews

Gene locus JW3748 in contig AP009048_GR.
Gene locus b3775 in contig U00096_GR.

KEGG

ecj:JW3748.
eco:b3775.

PATRIC

32123045. VBIEscCol129921_3892.

Organism-specific databases

EchoBASE

EB2256.

EcoGene

EG12352. ppiC.

Phylogenomic databases

eggNOG

COG0760.

GeneTree

EBGT00050000010660.

HOGENOM

HBG526275.

OMA

SCELLKP.

PhylomeDB

P0A9L5.

ProtClustDB

PRK15441.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12352-MONOMER.
MetaCyc:EG12352-MONOMER.

Gene expression databases

Genevestigator

P0A9L5.

Family and domain databases

InterPro

IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
[Graphical view]

KO

K03769.

Pfam

PF00639. Rotamase. 1 hit.
[Graphical view]

PROSITE

PS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PPIC_ECOLI

Accession

Primary (citable) accession number: P0A9L5
Secondary accession number(s): P39159, Q2M884

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program