P0A6F5 (CH60_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60 kDa chaperonin

Alternative name(s):
GroEL protein
Protein Cpn60

Gene names

Name:	groL
Synonyms:	groEL, mopA
Ordered Locus Names:	b4143, JW4103

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	548 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	Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. HAMAP MF_00600 Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell. HAMAP MF_00600
Subunit structure	Oligomer of 14 subunits composed of two stacked rings of 7 subunits.
Subcellular location	Cytoplasm HAMAP MF_00600.
Post-translational modification	Phosphorylated reversibly during heat shock. Ref.10
Miscellaneous	This protein shows ATPase activity. HAMAP MF_00600
Sequence similarities	Belongs to the chaperonin (HSP60) family.
Caution	Was originally (Ref.6) designated as the ams protein.
Sequence caution	The sequence AAA23934.1 differs from that shown. Reason: Frameshift at positions 424 and 455.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW phage assembly Inferred from mutant phenotype. Source: EcoliWiki protein refolding Inferred from electronic annotation. Source: InterPro response to heat Inferred from expression pattern. Source: EcoliWiki
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay Ref.17. Source: EcoCyc ATPase activity Inferred from direct assay. Source: EcoCyc identical protein binding Inferred from physical interaction. Source: IntAct unfolded protein binding Inferred from mutant phenotype. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-543750,EBI-543750
aceE	P0AFG8	2	EBI-543750,EBI-542683
ACT1	P60010	5	EBI-543750,EBI-2169	From a different organism.
cho	P76213	2	EBI-543750,EBI-545155
groS	P0A6F9	15	EBI-543750,EBI-369169
hyfG	P77329	3	EBI-543750,EBI-548413
malE	P0AEX9	3	EBI-543750,EBI-369910
mlaF	P63386	3	EBI-543750,EBI-561408
recF	P0A7H0	3	EBI-543750,EBI-556839
rfbC	P37745	2	EBI-543750,EBI-557071
ulaR	P0A9W0	3	EBI-543750,EBI-560926
uspG	P39177	4	EBI-543750,EBI-561722
ybbL	P77279	2	EBI-543750,EBI-560090
yhbU	P45527	3	EBI-543750,EBI-561157

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 548

547

60 kDa chaperonin HAMAP MF_00600

PRO_0000063358

Amino acid modifications

Modified residue

117

1

N6-acetyllysine Ref.12

Experimental info

Sequence conflict

83 – 86

4

DAAG → GALQ in CAA30739. Ref.5

Sequence conflict

262

1

L → A in CAA30698. Ref.1

Sequence conflict

267

1

M → I in CAA30698. Ref.1

Sequence conflict

343

1

Q → R in AAA23934. Ref.6

Secondary structure

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548

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

9 – 28

20

Beta strand

37 – 40

4

Beta strand

43 – 46

4

Beta strand

48 – 50

3

Helix

53 – 59

7

Helix

65 – 85

21

Helix

89 – 108

20

Helix

113 – 134

22

Helix

141 – 151

11

Helix

156 – 169

14

Beta strand

173 – 178

6

Beta strand

181 – 184

4

Beta strand

193 – 196

4

Helix

202 – 204

3

Turn

208 – 210

3

Beta strand

211 – 217

7

Beta strand

219 – 227

9

Helix

230 – 243

14

Beta strand

247 – 254

8

Helix

256 – 267

12

Beta strand

273 – 277

5

Beta strand

279 – 281

3

Helix

283 – 296

14

Helix

309 – 311

3

Helix

314 – 316

3

Beta strand

317 – 325

9

Beta strand

330 – 335

6

Helix

339 – 354

16

Helix

359 – 374

16

Beta strand

377 – 380

4

Helix

386 – 409

24

Beta strand

411 – 413

3

Turn

414 – 416

3

Helix

417 – 425

9

Turn

426 – 428

3

Helix

434 – 446

13

Helix

449 – 457

9

Helix

462 – 471

10

Beta strand

476 – 479

4

Turn

480 – 483

4

Beta strand

484 – 487

4

Turn

488 – 492

5

Beta strand

494 – 496

3

Helix

497 – 515

19

Beta strand

517 – 523

7

Sequences

	Sequence		Length	Mass (Da)
	P0A6F5 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CD3A0FB505F74AD1	FASTA	548	57,329
	10 20 30 40 50 60 MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI 70 80 90 100 110 120 ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI 130 140 150 160 170 180 DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG 190 200 210 220 230 240 TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV 250 260 270 280 290 300 AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 310 320 330 340 350 360 ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY 370 380 390 400 410 420 DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI 430 440 450 460 470 480 RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA 490 500 510 520 530 540 ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homologous plant and bacterial proteins chaperone oligomeric protein assembly." Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., Georgopoulos C., Hendrix R.W., Ellis R.J. Nature 333:330-334(1988) [PubMed: 2897629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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.
[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]. 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]	"Control of cell division by sex factor F in Escherichia coli. III. Participation of the groES (mopB) gene of the host bacteria." Miki T., Orita T., Furuno M., Horiuchi T. J. Mol. Biol. 201:327-338(1988) [PubMed: 2901493] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
[6]	"Cloning, sequence analysis, and expression of alteration of the mRNA stability gene (ams+) of Escherichia coli." Chanda P.K., Ono M., Kuwano M., Kung H.-F. J. Bacteriol. 161:446-449(1985) [PubMed: 2578448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-495.
[7]	"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 2-22. Strain: K12 / EMG2.
[8]	Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"The reaction of GroEL (cpn 60) with the ATP analogue 2',3' dialdehyde ATP." Thomson G.J., Coggins J.R., Price N.C. FEBS Lett. 336:19-22(1993) [PubMed: 7903255] [Abstract] Cited for: PROTEIN SEQUENCE OF 455-519.
[10]	"Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation." Sherman M.Y., Goldberg A.L. Nature 357:167-169(1992) [PubMed: 1349729] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"Residues in chaperonin GroEL required for polypeptide binding and release." Fenton W.A., Kashi Y., Furtak K., Horwich A.L. Nature 371:614-619(1994) [PubMed: 7935796] [Abstract] Cited for: MUTAGENESIS.
[12]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[13]	"The crystal structure of the bacterial chaperonin GroEL at 2.8 A." Braig K., Otwinowski Z., Hegde R.S., Boisvert D.C., Joachimiak A., Horwich A.L., Sigler P.B. Nature 371:578-586(1994) [PubMed: 7935790] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[14]	"Conformational variability in the refined structure of the chaperonin GroEL at 2.8-A resolution." Braig K., Adams P.D., Bruenger A.T. Nat. Struct. Biol. 2:1083-1094(1995) [PubMed: 8846220] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[15]	"The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S." Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B. Nat. Struct. Biol. 3:170-177(1996) [PubMed: 8564544] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[16]	"Chaperone activity and structure of monomeric polypeptide binding domains of GroEL." Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., Fersht A.R. Proc. Natl. Acad. Sci. U.S.A. 93:15024-15029(1996) [PubMed: 8986757] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[17]	"The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex." Xu Z., Horwich A.L., Sigler P.B. Nature 388:741-750(1997) [PubMed: 9285585] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[18]	"The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity." Chen L., Sigler P.B. Cell 99:757-768(1999) [PubMed: 10619429] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 192-337.
[19]	"Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions." Kiser P.D., Lodowski D.T., Palczewski K. Acta Crystallogr. F 63:457-461(2007) [PubMed: 17554162] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07850 Genomic DNA. Translation: CAA30698.1.
U14003 Genomic DNA. Translation: AAA97042.1.
U00096 Genomic DNA. Translation: AAC77103.1.
AP009048 Genomic DNA. Translation: BAE78145.1.
X07899 Genomic DNA. Translation: CAA30739.1.
M11294 Genomic DNA. Translation: AAA23934.1. Frameshift.

PIR

BVECGL. S56371.

RefSeq

NP_418567.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AON	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
1DK7	X-ray	2.02	A/B	191-336	[»]
1DKD	X-ray	2.10	A/B/C/D	191-336	[»]
1FY9	X-ray	2.20	A	191-376	[»]
1FYA	X-ray	2.20	A	191-376	[»]
1GR5	electron microscopy	7.90	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
1GRL	X-ray	2.80	A/B/C/D/E/F/G	1-548	[»]
1GRU	electron microscopy	12.50	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
1J4Z	X-ray	3.52	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
1JON	X-ray	2.50	A	191-345	[»]
1KID	X-ray	1.70	A	191-375	[»]
1KP8	X-ray	2.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
1KPO	X-ray	3.52	1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z	2-547	[»]
1LA1	X-ray	2.06	A	188-379	[»]
1MNF	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
1OEL	X-ray	2.80	A/B/C/D/E/F/G	2-548	[»]
1PCQ	X-ray	2.81	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-524	[»]
1PF9	X-ray	2.99	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-525	[»]
1SS8	X-ray	2.70	A/B/C/D/E/F/G	2-524	[»]
1SVT	X-ray	2.81	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-524	[»]
1SX3	X-ray	2.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-525	[»]
1SX4	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-524	[»]
1XCK	X-ray	2.92	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
2C7C	electron microscopy	7.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
2C7D	electron microscopy	8.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
2C7E	electron microscopy	9.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
2CGT	electron microscopy	8.20	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-547	[»]
2EU1	X-ray	3.29	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-548	[»]
2NWC	X-ray	3.02	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-548	[»]
2YEY	X-ray	3.30	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-525	[»]
3C9V	electron microscopy	4.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-527	[»]
3CAU	electron microscopy	4.20	A/B/C/D/E/F/G/H/I/J/K/L/M/N	2-527	[»]

ProteinModelPortal

P0A6F5.

SMR

P0A6F5. Positions 2-525.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-339N.

IntAct

P0A6F5. 690 interactions.

MINT

MINT-5232496.

2D gel databases

SWISS-2DPAGE

P0A6F5.

2DBase-Ecoli

P0A6F5.

ECO2DBASE

B056.5. 6TH EDITION.

Proteomic databases

PRIDE

P0A6F5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003358; EBESCP00000003358; EBESCG00000002749.
EBESCT00000017770; EBESCP00000017061; EBESCG00000016826.

GeneID

948665.

GenomeReviews

Gene locus JW4103 in contig AP009048_GR.
Gene locus b4143 in contig U00096_GR.

KEGG

ecj:JW4103.
eco:b4143.

PATRIC

32123855. VBIEscCol129921_4275.

Organism-specific databases

EchoBASE

EB0594.

EcoGene

EG10599. groL.

Phylogenomic databases

eggNOG

COG0459.

GeneTree

EBGT00050000009756.

HOGENOM

HBG625289.

OMA

DKPAAGM.

PhylomeDB

P0A6F5.

ProtClustDB

PRK00013.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10599-MONOMER.

Gene expression databases

Genevestigator

P0A6F5.

Family and domain databases

HAMAP

MF_00600. CH60.
[Tree]

InterPro

IPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
[Graphical view]

KO

K04077.

PANTHER

PTHR11353. Cpn60/TCP-1. 1 hit.

Pfam

PF00118. Cpn60_TCP1. 1 hit.
[Graphical view]

PRINTS

PR00298. CHAPERONIN60.

SUPFAM

SSF48592. GroEL-ATPase. 1 hit.

TIGRFAMs

TIGR02348. GroEL. 1 hit.

PROSITE

PS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CH60_ECOLI

Accession

Primary (citable) accession number: P0A6F5
Secondary accession number(s): P06139, Q2M6G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program