P43773 (HSLU_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent protease ATPase subunit HslU

Alternative name(s):
Unfoldase HslU

Gene names

Name:	hslU
Ordered Locus Names:	HI_0497

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. HAMAP-Rule MF_00249
Subunit structure	A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ClpX chaperone family. HslU subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC protein unfolding Inferred from electronic annotation. Source: HAMAP
Cellular_component	HslUV protease complex Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP ATPase activity Inferred from electronic annotation. Source: HAMAP peptidase activity, acting on L-amino acid peptides Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hslV	P43772	4	EBI-1030296,EBI-1030290

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 444

444

ATP-dependent protease ATPase subunit HslU HAMAP-Rule MF_00249

PRO_0000160508

Regions

Nucleotide binding

60 – 65

6

ATP HAMAP-Rule MF_00249

Nucleotide binding

306 – 309

4

ATP HAMAP-Rule MF_00249

Sites

Binding site

18

1

ATP; via amide nitrogen and carbonyl oxygen

Binding site

257

1

ATP By similarity

Binding site

322

1

ATP By similarity

Binding site

394

1

ATP By similarity

Secondary structure

1

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444

Helix Strand Turn

Details...

Helix

6 – 14

9

Helix

21 – 39

19

Turn

42 – 47

6

Beta strand

53 – 56

4

Beta strand

58 – 62

5

Helix

63 – 73

11

Beta strand

78 – 82

5

Helix

83 – 86

4

Helix

92 – 94

3

Helix

97 – 117

21

Beta strand

123 – 128

6

Helix

228 – 230

3

Beta strand

231 – 234

4

Helix

237 – 251

15

Beta strand

253 – 257

5

Helix

259 – 262

4

Beta strand

269 – 271

3

Helix

272 – 287

16

Beta strand

290 – 293

4

Beta strand

296 – 299

4

Helix

300 – 302

3

Beta strand

304 – 309

6

Beta strand

312 – 314

3

Helix

316 – 318

3

Helix

321 – 324

4

Beta strand

329 – 332

4

Helix

338 – 346

9

Helix

352 – 361

10

Turn

362 – 364

3

Beta strand

366 – 369

4

Helix

371 – 387

17

Helix

392 – 394

3

Helix

395 – 410

16

Helix

411 – 413

3

Beta strand

418 – 421

4

Helix

423 – 430

8

Turn

431 – 435

5

Helix

437 – 443

7

Sequences

	Sequence		Length	Mass (Da)
	P43773 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: C346EA478E4094CE	FASTA	444	49,372
	10 20 30 40 50 60 MSEMTPREIV SELDQHIIGQ ADAKRAVAIA LRNRWRRMQL QEPLRHEVTP KNILMIGPTG 70 80 90 100 110 120 VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDSAMKL VRQQEIAKNR 130 140 150 160 170 180 ARAEDVAEER ILDALLPPAK NQWGEVENHD SHSSTRQAFR KKLREGQLDD KEIEIDVSAG 190 200 210 220 230 240 VSMGVEIMAP PGMEEMTNQL QSLFQNLGSD KTKKRKMKIK DALKALIDDE AAKLINPEEL 250 260 270 280 290 300 KQKAIDAVEQ NGIVFIDEID KICKKGEYSG ADVSREGVQR DLLPLVEGST VSTKHGMVKT 310 320 330 340 350 360 DHILFIASGA FQVARPSDLI PELQGRLPIR VELTALSAAD FERILTEPHA SLTEQYKALM 370 380 390 400 410 420 ATEGVNIAFT TDAVKKIAEA AFRVNEKTEN IGARRLHTVM ERLMDKISFS ASDMNGQTVN 430 440 IDAAYVADAL GEVVENEDLS RFIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Crystal and solution structures of an HslUV protease-chaperone complex." Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., McKay D.B. Cell 103:633-643(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 2-175 IN COMPLEX WITH HSLV AND ATP.
[3]	"Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning." Trame C.B., McKay D.B. Acta Crystallogr. D 57:1079-1090(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ADP AND SULFATE.
[4]	"Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome." Kwon A.-R., Kessler B.M., Overkleeft H.S., McKay D.B. J. Mol. Biol. 330:185-195(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLV; MAGNESIUM; ADP AND INHIBITOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42023 Genomic DNA. Translation: AAC22154.1.

RefSeq

NP_438655.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G3I	X-ray	3.41	A/B/C/D/E/F/S/T/U/V/W/X	1-444	[»]
1G41	X-ray	2.30	A	1-444	[»]
1IM2	X-ray	2.80	A	1-444	[»]
1KYI	X-ray	3.10	A/B/C/D/E/F/S/T/U/V/W/X	1-444	[»]
1OFH	X-ray	2.50	A/B/C	1-444	[»]
1OFI	X-ray	3.20	A/B/C	1-444	[»]

ProteinModelPortal

P43773.

SMR

P43773. Positions 1-444.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6175N.

IntAct

P43773. 1 interaction.

STRING

71421.HI0497.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC22154; AAC22154; HI_0497.

GeneID

950614.

KEGG

hin:HI0497.

PATRIC

20189545. VBIHaeInf48452_0515.

Phylogenomic databases

eggNOG

COG1220.

KO

K03667.

OMA

KYGMIKT.

ProtClustDB

PRK05201.

Family and domain databases

HAMAP

MF_00249. HslU.

InterPro

IPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
[Graphical view]

PANTHER

PTHR11262:SF3. PTHR11262:SF3. 1 hit.

Pfam

PF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]

SMART

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

TIGRFAMs

TIGR00390. hslU. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P43773.

Entry information

Entry name

HSLU_HAEIN

Accession

Primary (citable) accession number: P43773

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program