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Protein

ATP-dependent protease ATPase subunit HslU

Gene

hslU

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181ATP; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei257 – 2571ATPBy similarity
Binding sitei322 – 3221ATPBy similarity
Binding sitei394 – 3941ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi60 – 656ATP1 Publication
Nucleotide bindingi306 – 3094ATP1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent protease ATPase subunit HslU
Alternative name(s):
Unfoldase HslU
Gene namesi
Name:hslU
Ordered Locus Names:HI_0497
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444ATP-dependent protease ATPase subunit HslUPRO_0000160508Add
BLAST

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
hslVP437724EBI-1030296,EBI-1030290

Protein-protein interaction databases

DIPiDIP-6175N.
IntActiP43773. 1 interaction.
STRINGi71421.HI0497.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 149Combined sources
Helixi21 – 3919Combined sources
Turni42 – 476Combined sources
Beta strandi53 – 564Combined sources
Beta strandi58 – 625Combined sources
Helixi63 – 7311Combined sources
Beta strandi78 – 825Combined sources
Helixi83 – 864Combined sources
Helixi92 – 943Combined sources
Helixi97 – 11721Combined sources
Beta strandi123 – 1286Combined sources
Helixi228 – 2303Combined sources
Beta strandi231 – 2344Combined sources
Helixi237 – 25115Combined sources
Beta strandi253 – 2575Combined sources
Helixi259 – 2624Combined sources
Beta strandi269 – 2713Combined sources
Helixi272 – 28716Combined sources
Beta strandi290 – 2934Combined sources
Beta strandi296 – 2994Combined sources
Helixi300 – 3023Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi312 – 3143Combined sources
Helixi316 – 3183Combined sources
Helixi321 – 3244Combined sources
Beta strandi329 – 3324Combined sources
Helixi338 – 3469Combined sources
Helixi352 – 36110Combined sources
Turni362 – 3643Combined sources
Beta strandi366 – 3694Combined sources
Helixi371 – 38717Combined sources
Helixi392 – 3943Combined sources
Helixi395 – 41016Combined sources
Helixi411 – 4133Combined sources
Beta strandi418 – 4214Combined sources
Helixi423 – 4308Combined sources
Turni431 – 4355Combined sources
Helixi437 – 4437Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G3IX-ray3.41A/B/C/D/E/F/S/T/U/V/W/X1-444[»]
1G41X-ray2.30A1-444[»]
1IM2X-ray2.80A1-444[»]
1KYIX-ray3.10A/B/C/D/E/F/S/T/U/V/W/X1-444[»]
1OFHX-ray2.50A/B/C1-107[»]
A/B/C244-444[»]
1OFIX-ray3.20A/B/C1-107[»]
A/B/C244-444[»]
ProteinModelPortaliP43773.
SMRiP43773. Positions 1-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43773.

Family & Domainsi

Sequence similaritiesi

Belongs to the ClpX chaperone family. HslU subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105C4N. Bacteria.
COG1220. LUCA.
KOiK03667.
OMAiRLHTTIE.
OrthoDBiEOG6NPM7G.
PhylomeDBiP43773.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00249. HslU.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF3. PTHR11262:SF3. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00390. hslU. 1 hit.

Sequencei

Sequence statusi: Complete.

P43773-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEMTPREIV SELDQHIIGQ ADAKRAVAIA LRNRWRRMQL QEPLRHEVTP
60 70 80 90 100
KNILMIGPTG VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII
110 120 130 140 150
RDLTDSAMKL VRQQEIAKNR ARAEDVAEER ILDALLPPAK NQWGEVENHD
160 170 180 190 200
SHSSTRQAFR KKLREGQLDD KEIEIDVSAG VSMGVEIMAP PGMEEMTNQL
210 220 230 240 250
QSLFQNLGSD KTKKRKMKIK DALKALIDDE AAKLINPEEL KQKAIDAVEQ
260 270 280 290 300
NGIVFIDEID KICKKGEYSG ADVSREGVQR DLLPLVEGST VSTKHGMVKT
310 320 330 340 350
DHILFIASGA FQVARPSDLI PELQGRLPIR VELTALSAAD FERILTEPHA
360 370 380 390 400
SLTEQYKALM ATEGVNIAFT TDAVKKIAEA AFRVNEKTEN IGARRLHTVM
410 420 430 440
ERLMDKISFS ASDMNGQTVN IDAAYVADAL GEVVENEDLS RFIL
Length:444
Mass (Da):49,372
Last modified:November 1, 1995 - v1
Checksum:iC346EA478E4094CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22154.1.
RefSeqiNP_438655.1. NC_000907.1.
WP_010868991.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22154; AAC22154; HI_0497.
GeneIDi950614.
KEGGihin:HI0497.
PATRICi20189545. VBIHaeInf48452_0515.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22154.1.
RefSeqiNP_438655.1. NC_000907.1.
WP_010868991.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G3IX-ray3.41A/B/C/D/E/F/S/T/U/V/W/X1-444[»]
1G41X-ray2.30A1-444[»]
1IM2X-ray2.80A1-444[»]
1KYIX-ray3.10A/B/C/D/E/F/S/T/U/V/W/X1-444[»]
1OFHX-ray2.50A/B/C1-107[»]
A/B/C244-444[»]
1OFIX-ray3.20A/B/C1-107[»]
A/B/C244-444[»]
ProteinModelPortaliP43773.
SMRiP43773. Positions 1-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6175N.
IntActiP43773. 1 interaction.
STRINGi71421.HI0497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22154; AAC22154; HI_0497.
GeneIDi950614.
KEGGihin:HI0497.
PATRICi20189545. VBIHaeInf48452_0515.

Phylogenomic databases

eggNOGiENOG4105C4N. Bacteria.
COG1220. LUCA.
KOiK03667.
OMAiRLHTTIE.
OrthoDBiEOG6NPM7G.
PhylomeDBiP43773.

Miscellaneous databases

EvolutionaryTraceiP43773.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00249. HslU.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF3. PTHR11262:SF3. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00390. hslU. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiHSLU_HAEIN
AccessioniPrimary (citable) accession number: P43773
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 11, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.