Reviewed, UniProtKB/Swiss-Prot P0A6H5 (HSLU_ECOLI)

Names and origin

Protein names

Recommended name:
    ATP-dependent hsl protease ATP-binding subunit hslU
Alternative name(s):
    Heat shock protein hslU

Gene names

Name:	hslU
Synonyms:	htpI
Ordered Locus Names:	b3931, JW3902

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Chaperone subunit of a proteasome-like degradation complex. HAMAP MF_00249
Subunit structure	A double ring-shaped homohexamer of hslV is capped on each side by a ring-shaped hslU homohexamer. HAMAP MF_00249
Subcellular location	Cytoplasm. HAMAP MF_00249
Sequence similarities	Belongs to the clpX chaperone family. HslU subfamily.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	HslUV protease complex Inferred from electronic annotation. Source: InterPro membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP ATPase activity Inferred from electronic annotation. Source: InterPro peptidase activity, acting on L-amino acid peptides Inferred from electronic annotation. Source: InterPro protein 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

Chain

1 – 443

443

ATP-dependent hsl protease ATP-binding subunit hslU HAMAP MF_00249

PRO_0000160500

Regions

Nucleotide binding

57 – 64

8

ATP Potential

Secondary structure

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443

Helix Strand Turn

Details...

Helix

6 – 13

8

Turn

14 – 16

3

Helix

21 – 37

17

Helix

42 – 45

4

Beta strand

53 – 56

4

Helix

63 – 74

12

Beta strand

78 – 82

5

Helix

83 – 86

4

Beta strand

89 – 91

3

Helix

98 – 118

21

Helix

120 – 129

10

Helix

132 – 135

4

Beta strand

148 – 152

5

Helix

153 – 164

12

Beta strand

171 – 173

3

Beta strand

214 – 216

3

Helix

218 – 233

16

Helix

236 – 250

15

Beta strand

252 – 256

5

Turn

257 – 261

5

Helix

269 – 286

18

Beta strand

289 – 292

4

Beta strand

295 – 298

4

Helix

299 – 301

3

Beta strand

303 – 308

6

Beta strand

311 – 313

3

Helix

315 – 317

3

Helix

320 – 324

5

Beta strand

328 – 331

4

Helix

337 – 345

9

Helix

351 – 360

10

Turn

361 – 363

3

Beta strand

365 – 368

4

Helix

370 – 386

17

Helix

393 – 409

17

Helix

410 – 413

4

Beta strand

417 – 420

4

Helix

422 – 434

13

Helix

436 – 439

4

Sequences

	Sequence		Length	Mass (Da)
	P0A6H5-1 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: D2188639EA9AEF4C	FASTA	443	49,594
	10 20 30 40 50 60 MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP KNILMIGPTG 70 80 90 100 110 120 VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRVQAIEKNR 130 140 150 160 170 180 YRAEELAEER ILDVLIPPAK NNWGQTEQQQ EPSAARQAFR KKLREGQLDD KEIEIDLAAA 190 200 210 220 230 240 PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK 250 260 270 280 290 300 QDAIDAVEQH GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD 310 320 330 340 350 360 HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS ITVQYKALMA 370 380 390 400 410 420 TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE RLMEEISYDA SDLSGQNITI 430 440 DADYVSKHLD ALVADEDLSR FIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli." Chuang S.E., Burland V., Plunkett G. III, Daniels D.L., Blattner F.R. Gene 134:1-6(1993) [PubMed: 8244018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed: 8346018] [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]	"Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis." Yoo S.J., Kim H.H., Shin D.H., Lee C.S., Seong I.S., Seol J.H., Shimbara N., Tanaka K., Chung C.H. J. Biol. Chem. 273:22929-22935(1998) [PubMed: 9722513] [Abstract] Cited for: MUTAGENESIS.
[6]	"The structures of HslU and the ATP-dependent protease HslU-HslV." Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R. Nature 403:800-805(2000) [PubMed: 10693812] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEX WITH HSLV.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L19201 Genomic DNA. Translation: AAB03063.1.
U00096 Genomic DNA. Translation: AAC76913.1.
AP009048 Genomic DNA. Translation: BAE77379.1.

PIR

JT0761.

RefSeq

AP_003878.1.
NP_418366.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DO0	X-ray	3.00	A/B/C/D/E/F	2-443	[»]
1DO2	X-ray	4.00	A/B/C/D	2-443	[»]
1E94	X-ray	2.80	E/F	2-443	[»]
1G4A	X-ray	3.00	E/F	1-443	[»]
1G4B	X-ray	7.00	E/F/K/L	1-443	[»]
1HQY	X-ray	2.80	E/F	2-443	[»]
1HT1	X-ray	2.80	E/F/G/I	2-443	[»]
1HT2	X-ray	2.80	E/F/G/H	2-443	[»]
1YYF	X-ray	4.16	A/B	1-443	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A6H5.

2-D gel databases

SWISS-2DPAGE

P0A6H5.

ECO2DBASE

D048.5. 6TH EDITION.

Genome annotation databases

GeneID

948430.

GenomeReviews

Gene locus JW3902 in contig AP009048_GR.
Gene locus b3931 in contig U00096_GR.

KEGG

ecj:JW3902.
eco:b3931.

Organism-specific databases

EchoBASE

EB1827.

EcoGene

EG11881. hslU.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6H5.

OMA

TDHVLFI.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11881-MON.

Gene expression databases

Genevestigator

P0A6H5.

Family and domain databases

HAMAP

MF_00249.
[Tree]

InterPro

IPR003593. ATPase_AAA+_core.
IPR013093. ATPase_AAA-2.
IPR004491. HslU.
[Graphical view]

PANTHER

PTHR11262:SF3. HslU. 1 hit.

Pfam

PF07724. AAA_2. 2 hits.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00390. hslU. 1 hit.

ProtoNet

Search...

Entry information

Entry name

HSLU_ECOLI

Accession

Primary (citable) accession number: P0A6H5
Secondary accession number(s): P32168, Q2M8M7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)