P0A6H1 (CLPX_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent Clp protease ATP-binding subunit ClpX

Gene names

Name:	clpX
Synonyms:	lopC
Ordered Locus Names:	b0438, JW0428

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	424 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	ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP. HAMAP-Rule MF_00175
Subunit structure	Heterodimer of ClpP and ClpX.
Induction	By heat shock. HAMAP-Rule MF_00175
Sequence similarities	Belongs to the ClpX chaperone family.

Ontologies

Keywords
Biological process	Stress response
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: HAMAP response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from direct assay PubMed 9575205. Source: EcoCyc nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 424

423

ATP-dependent Clp protease ATP-binding subunit ClpX HAMAP-Rule MF_00175

PRO_0000160352

Regions

Zinc finger

15 – 40

26

C4-type HAMAP-Rule MF_00175

Nucleotide binding

119 – 126

8

ATP Potential

Experimental info

Sequence conflict

268 – 274

7

IGFGATV → HWCWRSG in CAA80816. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

424

Helix Strand Turn

Details...

Turn

16 – 18

3

Turn

22 – 24

3

Beta strand

28 – 30

3

Beta strand

35 – 37

3

Helix

38 – 49

12

Helix

67 – 77

11

Helix

82 – 100

19

Beta strand

105 – 107

3

Beta strand

115 – 118

4

Helix

125 – 135

11

Beta strand

140 – 144

5

Helix

145 – 148

4

Helix

152 – 158

7

Helix

160 – 168

9

Turn

169 – 171

3

Helix

173 – 178

6

Beta strand

180 – 184

5

Helix

186 – 189

4

Helix

201 – 216

16

Beta strand

242 – 249

8

Helix

254 – 262

9

Helix

283 – 288

6

Helix

292 – 298

7

Helix

302 – 305

4

Beta strand

310 – 313

4

Helix

319 – 327

9

Helix

333 – 342

10

Turn

343 – 345

3

Beta strand

347 – 350

4

Helix

352 – 364

13

Turn

368 – 371

4

Helix

372 – 385

14

Turn

387 – 389

3

Beta strand

393 – 397

5

Helix

399 – 402

4

Beta strand

410 – 412

3

Sequences

	Sequence		Length	Mass (Da)
	P0A6H1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9DEF1B0786E42B6F	FASTA	424	46,356
	10 20 30 40 50 60 MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE EIKEVAPHRE 70 80 90 100 110 120 RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR NGDTSNGVEL GKSNILLIGP 130 140 150 160 170 180 TGSGKTLLAE TLARLLDVPF TMADATTLTE AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI 190 200 210 220 230 240 VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT 250 260 270 280 290 300 SKILFICGGA FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL 310 320 330 340 350 360 IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF RDEALDAIAK 370 380 390 400 410 420 KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE SVIDGQSKPL LIYGKPEAQQ ASGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities." Gottesman S., Clark W.P., de Crecy-Lagard V., Maurizi M.R. J. Biol. Chem. 268:22618-22626(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	Yoo S., Seol J., Ha D., Goldberg A., Chung C. Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[6]	"Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli." Wojtkowiak D., Georgopoulos C., Zylicz M. J. Biol. Chem. 268:22609-22617(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-25, CHARACTERIZATION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone." Wawrzynow A., Wojtkowiak D., Marszalek J., Banecki B., Jonsen M., Graves B., Georgopoulos C., Zylicz M. EMBO J. 14:1867-1877(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Solution structure of the dimeric zinc binding domain of the chaperone ClpX." Donaldson L.W., Wojtyra U., Houry W.A. J. Biol. Chem. 278:48991-48996(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-61.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L18867 Unassigned DNA. Translation: AAA16116.1.
Z23278 Genomic DNA. Translation: CAA80816.1.
U82664 Genomic DNA. Translation: AAB40194.1.
U00096 Genomic DNA. Translation: AAC73541.1.
AP009048 Genomic DNA. Translation: BAE76218.1.

PIR

A48709.

RefSeq

NP_414972.1. NC_000913.2.
YP_488730.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OVX	NMR	-	A/B	2-61	[»]
2DS5	X-ray	1.50	A/B	2-51	[»]
2DS6	X-ray	2.00	A/B	2-51	[»]
2DS7	X-ray	2.50	A	2-51	[»]
2DS8	X-ray	1.60	A/B	2-51	[»]
3HTE	X-ray	4.03	A/B/C/D/E/F	62-424	[»]
3HWS	X-ray	3.25	A/B/C/D/E/F	62-424	[»]

ProteinModelPortal

P0A6H1.

SMR

P0A6H1. Positions 9-52, 63-413.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35907N.

IntAct

P0A6H1. 31 interactions.

STRING

511145.b0438.

Proteomic databases

PaxDb

P0A6H1.

PRIDE

P0A6H1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73541; AAC73541; b0438.
BAE76218; BAE76218; BAE76218.

GeneID

12931741.
945083.

KEGG

ecj:Y75_p0426.
eco:b0438.

PATRIC

32116029. VBIEscCol129921_0456.

Organism-specific databases

EchoBASE

EB0157.

EcoGene

EG10159. clpX.

Phylogenomic databases

eggNOG

COG1219.

HOGENOM

HOG000010093.

KO

K03544.

OMA

SDLELEH.

ProtClustDB

PRK05342.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10159-MONOMER.
ECOL316407:JW0428-MONOMER.
MetaCyc:EG10159-MONOMER.

Gene expression databases

Genevestigator

P0A6H1.

Family and domain databases

HAMAP

MF_00175. ClpX.

InterPro

IPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR019489. Clp_ATPase_C.
IPR004487. Clp_protease_ATP-bd_su_ClpX.
IPR010603. Znf_CppX_C4.
[Graphical view]

PANTHER

PTHR11262:SF4. PTHR11262:SF4. 1 hit.

Pfam

PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
PF06689. zf-C4_ClpX. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
SM00994. zf-C4_ClpX. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00382. clpX. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6H1.

Entry information

Entry name

CLPX_ECOLI

Accession

Primary (citable) accession number: P0A6H1
Secondary accession number(s): P33138, Q2MBY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program