P63284 (CLPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chaperone protein ClpB

Alternative name(s):
Heat shock protein F84.1

Gene names

Name:	clpB
Synonyms:	htpM
Ordered Locus Names:	b2592, JW2573

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	857 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. Ref.13 Ref.14 Ref.16
Subunit structure	Homohexamer. The oligomerization is ATP-dependent. Ref.12 Ref.17
Subcellular location	Cytoplasm Ref.10.
Induction	By heat shock and other environmental stresses.
Domain	The N-terminal domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer. Ref.13 Ref.14 Ref.16 Ref.21
Miscellaneous	One peptide binds per ClpB hexamer; the binding site is formed only upon ATP-driven oligomerization.
Sequence similarities	Belongs to the clpA/clpB family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein processing Inferred from electronic annotation. Source: InterPro response to heat Inferred from electronic annotation. Source: InterPro response to unfolded protein Inferred from direct assay PubMed 1400361. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-546182,EBI-546182

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform ClpB (identifier: P63284-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform ClpB-3 (identifier: P63284-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
     149-149: V → M

Note: ClpB-3 ATPase activity is not activated by proteins, as it is in ClpB.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 857

857

Chaperone protein ClpB

PRO_0000005491

Regions

Nucleotide binding

206 – 213

8

ATP 1

Nucleotide binding

605 – 612

8

ATP 2

Region

1 – 143

143

N-terminal

Region

159 – 340

182

NBD1

Region

341 – 545

205

Linker

Region

555 – 765

211

NBD2

Region

766 – 857

92

C-terminal

Coiled coil

391 – 525

135

By similarity

Amino acid modifications

Modified residue

96

1

N6-acetyllysine Ref.23

Modified residue

176

1

N6-acetyllysine Ref.23

Modified residue

640

1

N6-acetyllysine Ref.23

Natural variations

Alternative sequence

1 – 148

148

Missing in isoform ClpB-3.

VSP_018703

Alternative sequence

149

1

V → M in isoform ClpB-3.

VSP_018987

Experimental info

Mutagenesis

7

1

T → A: Loss of chaperone activity. Ref.19

Mutagenesis

84

1

S → A: No effect. Ref.19

Mutagenesis

93

1

L → Q: Loss of chaperone activity. Retains ATPase activity. Ref.25

Mutagenesis

97

1

L → Q: 75% decrease in chaperone activity; retains ATPase activity. Ref.25

Mutagenesis

103

1

D → A: Loss of chaperone activity. Ref.19

Mutagenesis

109

1

E → A: Loss of chaperone activity. Ref.19

Mutagenesis

110

1

L → Q: 30% decrease in chaperone activity; retains ATPase activity. Ref.25

Mutagenesis

212

1

K → T: Loss of ability to form oligomers even in the presence of ATP. Loss of chaperone activity. Ref.12 Ref.14 Ref.20

Mutagenesis

251

1

Y → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity. Ref.18

Mutagenesis

254

1

E → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity; when associated with A-257. Ref.18

Mutagenesis

257

1

E → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity; when associated with A-254. Ref.18

Mutagenesis

279

1

E → A: No effect on oligomerization. Ref.14

Mutagenesis

332

1

R → A: Loss of ability to form oligomers. Ref.14

Mutagenesis

543

1

W → F: No effect on chaperone activity or ability to form oligomers. Ref.14

Mutagenesis

611

1

K → T: No effect on ability to form oligomers. Loss of chaperone activity. Ref.12 Ref.14 Ref.20

Mutagenesis

678

1

E → A: No effect on oligomerization. Ref.14

Mutagenesis

756

1

R → A: No effect on oligomerization. Loss of ATPase activity. Ref.14

Mutagenesis

797

1

D → A: No effect. Ref.20

Mutagenesis

813 – 815

3

GAR → AAA: No effect on oligomerization. Ref.14 Ref.20

Mutagenesis

815

1

R → A: Loss of ability to form oligomers; loss of chaperone activity. Ref.20

Mutagenesis

819

1

R → A: Loss of ability to form oligomers; loss of chaperone activity. Ref.20

Mutagenesis

826

1

E → A: No effect. Ref.20

Sequence conflict

96 – 97

2

KL → NV in AAA24422. Ref.1

Sequence conflict

122

1

L → V in AAA24422. Ref.1

Secondary structure

1

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857

Helix Strand Turn

Details...

Helix

8 – 23

16

Beta strand

27 – 29

3

Helix

31 – 39

9

Helix

46 – 53

8

Helix

57 – 68

12

Helix

85 – 101

17

Beta strand

104 – 106

3

Helix

108 – 116

9

Helix

120 – 128

9

Helix

133 – 141

9

Helix

159 – 164

6

Beta strand

165 – 167

3

Helix

168 – 173

6

Helix

184 – 194

11

Beta strand

196 – 199

4

Beta strand

201 – 205

5

Helix

212 – 225

14

Helix

230 – 232

3

Beta strand

236 – 240

5

Helix

242 – 246

5

Turn

247 – 249

3

Helix

252 – 268

17

Turn

270 – 272

3

Beta strand

273 – 278

6

Helix

280 – 283

4

Helix

296 – 304

9

Beta strand

310 – 314

5

Helix

316 – 322

7

Turn

323 – 325

3

Helix

327 – 330

4

Beta strand

333 – 337

5

Helix

343 – 347

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform ClpB [UniParc]. Last modified October 11, 2004. Version 1. Checksum: FD38CD96B2F7C32A	FASTA	857	95,585
	10 20 30 40 50 60 MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL TSAGINAGQL 70 80 90 100 110 120 RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK RGDNFISSEL FVLAALESRG 130 140 150 160 170 180 TLADILKAAG ATTANITQAI EQMRGGESVN DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV 190 200 210 220 230 240 IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL 250 260 270 280 290 300 DMGALVAGAK YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK 310 320 330 340 350 360 PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL RGLKERYELH 370 380 390 400 410 420 HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE ELDRLDRRII 430 440 450 460 470 480 QLKLEQQALM KESDEASKKR LDMLNEELSD KERQYSELEE EWKAEKASLS GTQTIKAELE 490 500 510 520 530 540 QAKIAIEQAR RVGDLARMSE LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL 550 560 570 580 590 600 ARWTGIPVSR MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS 610 620 630 640 650 660 FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG 670 680 690 700 710 720 YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL 730 740 750 760 770 780 GSDLIQERFG ELDYAHMKEL VLGVVSHNFR PEFINRIDEV VVFHPLGEQH IASIAQIQLK 790 800 810 820 830 840 RLYKRLEERG YEIHISDEAL KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP 850 GKVIRLEVNE DRIVAVQ
	Isoform ClpB-3 [UniParc]. Checksum: 60270862D6198B55	FASTA	709	79,870
	10 20 30 40 50 60 MNDQGAEDQR QALKKYTIDL TERAEQGKLD PVIGRDEEIR RTIQVLQRRT KNNPVLIGEP 70 80 90 100 110 120 GVGKTAIVEG LAQRIINGEV PEGLKGRRVL ALDMGALVAG AKYRGEFEER LKGVLNDLAK 130 140 150 160 170 180 QEGNVILFID ELHTMVGAGK ADGAMDAGNM LKPALARGEL HCVGATTLDE YRQYIEKDAA 190 200 210 220 230 240 LERRFQKVFV AEPSVEDTIA ILRGLKERYE LHHHVQITDP AIVAAATLSH RYIADRQLPD 250 260 270 280 290 300 KAIDLIDEAA SSIRMQIDSK PEELDRLDRR IIQLKLEQQA LMKESDEASK KRLDMLNEEL 310 320 330 340 350 360 SDKERQYSEL EEEWKAEKAS LSGTQTIKAE LEQAKIAIEQ ARRVGDLARM SELQYGKIPE 370 380 390 400 410 420 LEKQLEAATQ LEGKTMRLLR NKVTDAEIAE VLARWTGIPV SRMMESEREK LLRMEQELHH 430 440 450 460 470 480 RVIGQNEAVD AVSNAIRRSR AGLADPNRPI GSFLFLGPTG VGKTELCKAL ANFMFDSDEA 490 500 510 520 530 540 MVRIDMSEFM EKHSVSRLVG APPGYVGYEE GGYLTEAVRR RPYSVILLDE VEKAHPDVFN 550 560 570 580 590 600 ILLQVLDDGR LTDGQGRTVD FRNTVVIMTS NLGSDLIQER FGELDYAHMK ELVLGVVSHN 610 620 630 640 650 660 FRPEFINRID EVVVFHPLGE QHIASIAQIQ LKRLYKRLEE RGYEIHISDE ALKLLSENGY 670 680 690 700 DPVYGARPLK RAIQQQIENP LAQQILSGEL VPGKVIRLEV NEDRIVAVQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes." Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M., Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T., Clark W.P., Ross B., Squires C.L., Maurizi M.R. Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32)." Kitagawa M., Wada C., Yoshioka S., Yura T. J. Bacteriol. 173:4247-4253(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-593. Strain: K12.
[6]	"Nucleotide sequence of the rrnG ribosomal RNA promoter region of Escherichia coli." Shen W.-F., Squires C., Squires C.L. Nucleic Acids Res. 10:3303-3313(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 753-857.
[7]	Ogura T., Tomoyasu T. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"ClpB proteins copurify with the anaerobic Escherichia coli reductase." Pontis E., Sun X.Y., Joernvall H., Krook M., Reichard P. Biochem. Biophys. Res. Commun. 180:1222-1226(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-14; 150-157; 355-364 AND 452-460.
[9]	"ClpB is the Escherichia coli heat shock protein F84.1." Squires C.L., Pedersen S., Ross B.M., Squires C. J. Bacteriol. 173:4254-4262(1991) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A HEAT SHOCK PROTEIN.
[10]	"Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products." Park S.K., Kim K.I., Woo K.M., Seol J.H., Tanaka K., Ichihara A., Ha D.B., Chung C.H. J. Biol. Chem. 268:20170-20174(1993) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE INITIATION, ATPASE ACTIVITY, SUBCELLULAR LOCATION.
[11]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[12]	"Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli." Kim K.I., Cheong G.-W., Park S.-C., Ha J.-S., Woo K.M., Choi S.J., Chung C.H. J. Mol. Biol. 303:655-666(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, MUTAGENESIS OF LYS-212 AND LYS-611.
[13]	"Structure and activity of ClpB from Escherichia coli. Role of the amino- and -carboxyl-terminal domains." Barnett M.E., Zolkiewska A., Zolkiewski M. J. Biol. Chem. 275:37565-37571(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF DOMAINS.
[14]	"Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity." Mogk A., Schlieker C., Strub C., Rist W., Weibezahn J., Bukau B. J. Biol. Chem. 278:17615-17624(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF DOMAINS, MUTAGENESIS OF LYS-212; GLU-279; ARG-332; TRP-543; LYS-611; GLU-678; ARG-756 AND 813-GLY--ARG-815. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[15]	"Characterization of a trap mutant of the AAA+ chaperone ClpB." Weibezahn J., Schlieker C., Bukau B., Mogk A. J. Biol. Chem. 278:32608-32617(2003) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING TO PROTEIN AGGREGATES, INTERACTION WITH DNAK. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[16]	"Structure and function of the middle domain of ClpB from Escherichia coli." Kedzierska S., Akoev V., Barnett M.E., Zolkiewski M. Biochemistry 42:14242-14248(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF MIDDLE DOMAIN.
[17]	"Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB." Akoev V., Gogol E.P., Barnett M.E., Zolkiewski M. Protein Sci. 13:567-574(2004) [PubMed] [Europe PMC] [Abstract] Cited for: OLIGOMERIZATION, NUCLEOTIDE-BINDING. Strain: K12 / MC1000 / ATCC 39531.
[18]	"Substrate recognition by the AAA+ chaperone ClpB." Schlieker C., Weibezahn J., Patzelt H., Tessarz P., Strub C., Zeth K., Erbse A., Schneider-Mergener J., Chin J.W., Schultz P.G., Bukau B., Mogk A. Nat. Struct. Mol. Biol. 11:607-615(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE-BINDING, MUTAGENESIS OF TYR-251; GLU-254 AND GLU-257. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[19]	"Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity." Liu Z., Tek V., Akoev V., Zolkiewski M. J. Mol. Biol. 321:111-120(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF THR-7; SER-84; ASP-103 AND GLU-109.
[20]	"Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli." Barnett M.E., Zolkiewski M. Biochemistry 41:11277-11283(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-212; LYS-611; ASP-797; ARG-815; ARG-819 AND GLU-826.
[21]	"Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB N-terminal domain." Li J., Sha B. Acta Crystallogr. D 57:1933-1935(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION OF N-TERMINAL DOMAIN.
[22]	"Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 nucleotide-binding domain 2 (NBD2)." Li J., Sha B. Acta Crystallogr. D 58:1030-1031(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION OF NBD2.
[23]	"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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-176 AND LYS-640, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[24]	"Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity." Li J., Sha B. J. Mol. Biol. 318:1127-1137(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-351.
[25]	"Crystal structure of the E. coli Hsp100 ClpB N-terminal domain." Li J., Sha B. Structure 11:323-328(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-142, MUTAGENESIS OF LEU-93; LEU-97 AND LEU-110.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29364 Genomic DNA. Translation: AAA24422.1.
U00096 Genomic DNA. Translation: AAC75641.1.
AP009048 Genomic DNA. Translation: BAA16476.1.
X57620 Genomic DNA. Translation: CAA40846.1.
V00350 Genomic DNA. Translation: CAA23639.1.
U50134 Genomic DNA. Translation: AAA92959.1.

PIR

D35905. C65037.

RefSeq

NP_417083.1. NC_000913.2.
YP_490816.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JBK	X-ray	1.80	A	159-351	[»]
1KHY	X-ray	1.95	A/B/C/D	1-148	[»]

ProteinModelPortal

P63284.

SMR

P63284. Positions 4-848.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35844N.

IntAct

P63284. 72 interactions.

MINT

MINT-1222117.

STRING

511145.b2592.

2D gel databases

SWISS-2DPAGE

P63284.

Proteomic databases

PaxDb

P63284.

PRIDE

P63284.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75641; AAC75641; b2592.
BAA16476; BAA16476; BAA16476.

GeneID

12931624.
947077.

KEGG

ecj:Y75_p2541.
eco:b2592.

PATRIC

32120587. VBIEscCol129921_2692.

Organism-specific databases

EchoBASE

EB0155.

EcoGene

EG10157. clpB.

Phylogenomic databases

eggNOG

COG0542.

HOGENOM

HOG000218211.

KO

K03695.

OMA

LIQDRFG.

ProtClustDB

PRK10865.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10157-MONOMER.
ECOL316407:JW2573-MONOMER.

Gene expression databases

Genevestigator

P63284.

Family and domain databases

Gene3D

1.10.1780.10. 1 hit.

InterPro

IPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR018368. Chaperonin_ClpA/B_CS.
IPR017730. Chaperonin_ClpB.
IPR001270. Chaprnin_ClpA/B.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR023150. Dbl_Clp-N.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]

PRINTS

PR00300. CLPPROTEASEA.

SMART

SM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03346. chaperone_ClpB. 1 hit.

PROSITE

PS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P63284.

Entry information

Entry name

CLPB_ECOLI

Accession

Primary (citable) accession number: P63284
Secondary accession number(s): P03815

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program