hslV

Functionⁱ

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.UniRule annotation7 Publications

Caution

PubMed:9013898 sequence is supposed to originate from rat but, based on sequence similarity, it seems that this is a case of bacterial contamination from E.coli.Curated

Catalytic activityⁱ

ATP-dependent cleavage of peptide bonds with broad specificity.UniRule annotation5 Publications

Activity regulationⁱ

Allosterically activated by HslU binding.Curated

Kineticsⁱ

Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.

K_M=
5.2 µM for Arc-MYL-st11 (at 37 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.17
  "Nucleotide-dependent substrate recognition by the AAA+ HslUV protease."
  Burton R.E., Baker T.A., Sauer R.T.
  Nat. Struct. Mol. Biol. 12:245-251(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Temperature dependenceⁱ

Optimum temperature is 55 degrees Celsius.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	2	UniRule annotation1 Publication	1
Metal bindingⁱ	157	Sodium; via carbonyl oxygen	1
Metal bindingⁱ	160	Sodium; via carbonyl oxygen	1
Metal bindingⁱ	163	Sodium; via carbonyl oxygen	1

GO - Molecular functionⁱ

ATP binding
Source: CAFA
Inferred from direct assayⁱ
- 10693812
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
magnesium ion binding
Source: CAFA
Inferred from direct assayⁱ
- 10693812
protein domain specific binding
Source: CAFA
Inferred from physical interactionⁱ
- 10693812
threonine-type endopeptidase activity
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 9257689

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

protein hexamerization
Source: CAFA
Inferred from direct assayⁱ
- 10693812
proteolysis
Source: CAFA
Inferred from direct assayⁱ
- 10693812
proteolysis involved in cellular protein catabolic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 9003766
response to heat
Source: EcoliWiki
Inferred from expression patternⁱ
- 8349564

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Allosteric enzyme, Hydrolase, Protease, Threonine protease
Biological process	Stress response
Ligand	Metal-binding, Sodium

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11676-MONOMER MetaCyc:EG11676-MONOMER
BRENDAⁱ	3.4.25.2 2026

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: ATP-dependent protease subunit HslVUniRule annotation (EC:3.4.25.2UniRule annotation) Alternative name(s): Heat shock protein HslVUniRule annotation
Gene namesⁱ	Name:hslVUniRule annotation Synonyms:htpO, yiiC Ordered Locus Names:b3932, JW3903
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11676 hslV

EcoGeneⁱ

EG11676 hslV

Subcellular locationⁱ

Cytoplasm

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323
HslUV protease complex
Source: CAFA
Inferred from direct assayⁱ
- 10693812
proteasome core complex Source: InterPro

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	2	T → S: 80% reduced protease activity in the absence of HslU. Almost no effect in the presence of HslU. 1 Publication	1
Mutagenesisⁱ	2	T → V: No protease activity. 1 Publication	1
Mutagenesisⁱ	3	T → S or V: 80% reduced protease activity. 1 Publication	1
Mutagenesisⁱ	6	S → A: No effect. 1 Publication	1
Mutagenesisⁱ	104	S → A: 50% reduced protease activity. 1 Publication	1
Mutagenesisⁱ	125	S → A: Almost no protease activity. 1 Publication	1
Mutagenesisⁱ	144	S → A: No effect. 1 Publication	1
Mutagenesisⁱ	160	C → A or S: No protease activity. Cannot form complexes with HslU. 1 Publication	1
Mutagenesisⁱ	173	S → A: Almost no protease activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed
ChainⁱPRO_0000148105	2 – 176	ATP-dependent protease subunit HslVAdd BLAST		175

Proteomic databases

EPDⁱ	P0A7B8
PaxDbⁱ	P0A7B8
PRIDEⁱ	P0A7B8

2D gel databases

SWISS-2DPAGEⁱ	P0A7B8

SWISS-2DPAGEⁱ

P0A7B8

Expressionⁱ

Inductionⁱ

By heat shock.UniRule annotation1 Publication

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.UniRule annotation1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-552265,EBI-552265
hslU	P0A6H5	16	EBI-552265,EBI-369317

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4261781, 287 interactors
ComplexPortalⁱ	CPX-2104 HslUV protease complex
Database of interacting proteins More...DIPⁱ	DIP-35866N
IntActⁱ	P0A7B8, 33 interactors
STRINGⁱ	316385.ECDH10B_4121

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 8	Combined sources	6
Beta strandⁱ	10 – 17	Combined sources	8
Beta strandⁱ	21 – 23	Combined sources	3
Beta strandⁱ	26 – 30	Combined sources	5
Beta strandⁱ	35 – 38	Combined sources	4
Turnⁱ	39 – 42	Combined sources	4
Beta strandⁱ	43 – 49	Combined sources	7
Helixⁱ	51 – 66	Combined sources	16
Turnⁱ	67 – 70	Combined sources	4
Helixⁱ	72 – 85	Combined sources	14
Helixⁱ	89 – 91	Combined sources	3
Beta strandⁱ	94 – 99	Combined sources	6
Beta strandⁱ	104 – 108	Combined sources	5
Turnⁱ	109 – 111	Combined sources	3
Beta strandⁱ	112 – 114	Combined sources	3
Turnⁱ	117 – 119	Combined sources	3
Beta strandⁱ	121 – 124	Combined sources	4
Helixⁱ	127 – 138	Combined sources	12
Helixⁱ	145 – 159	Combined sources	15
Beta strandⁱ	168 – 173	Combined sources	6

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A7B8
SMRⁱ	P0A7B8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A7B8

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the peptidase T1B family. HslV subfamily.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4108R5P Bacteria COG5405 LUCA
HOGENOMⁱ	HOG000064533
InParanoidⁱ	P0A7B8
KEGG Orthology (KO) More...KOⁱ	K01419
PhylomeDBⁱ	P0A7B8

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01913 protease_HslV, 1 hit
Gene3Dⁱ	3.60.20.10, 1 hit
HAMAPⁱ	MF_00248 HslV, 1 hit
InterProⁱ	View protein in InterPro IPR022281 ATP-dep_Prtase_HsIV_su IPR029055 Ntn_hydrolases_N IPR001353 Proteasome_sua/b IPR023333 Proteasome_suB-type
PANTHERⁱ	PTHR32194 PTHR32194, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00227 Proteasome, 1 hit
PIRSFⁱ	PIRSF039093 HslV, 1 hit
SUPFAMⁱ	SSF56235 SSF56235, 1 hit
TIGRFAMsⁱ	TIGR03692 ATP_dep_HslV, 1 hit
PROSITEⁱ	View protein in PROSITE PS51476 PROTEASOME_BETA_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P0A7B8-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG 
        60         70         80         90        100
TADAFTLFEL FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD 
       110        120        130        140        150
ETASLIITGN GDVVQPENDL IAIGSGGPYA QAAARALLEN TELSAREIAE 
       160        170 
KALDIAGDIC IYTNHFHTIE ELSYKA

Length:176

Mass (Da):19,093

Last modified:January 23, 2007 - v2

Checksum:ⁱ3B35E01F51486965

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L19201 Genomic DNA Translation: AAB03064.1 U00096 Genomic DNA Translation: AAC76914.1 AP009048 Genomic DNA Translation: BAE77378.1 D89965 mRNA Translation: BAA14040.1 Sequence problems. L14281 Genomic DNA No translation available.
PIRⁱ	JT0760
NCBI Reference Sequences More...RefSeqⁱ	NP_418367.1, NC_000913.3 WP_000208242.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76914; AAC76914; b3932 BAE77378; BAE77378; BAE77378
GeneIDⁱ	948429
KEGGⁱ	ecj:JW3903 eco:b3932
PATRICⁱ	fig\|1411691.4.peg.2773

Protein	Similar proteins		Species	Score	Length	Source
P0A7B8	ATP-dependent protease subunit HslV		ECO24		176	UniRef100_A7ZUE7
ATP-dependent protease subunit HslV		ECO27		176
ATP-dependent protease subunit HslV	)	ECO55		176
ATP-dependent protease subunit HslV		ECO57		176
ATP-dependent protease subunit HslV		ECO5E		176
+166

Protein	Similar proteins		Species	Score	Length	Source
P0A7B8	ATP-dependent protease subunit HslV		ECO24		176	UniRef90_A7ZUE7
ATP-dependent protease subunit HslV		ECO27		176
ATP-dependent protease subunit HslV	)	ECO55		176
ATP-dependent protease subunit HslV		ECO57		176
ATP-dependent protease subunit HslV		ECO5E		176
+223

Protein	Similar proteins		Species	Score	Length	Source
P0A7B8	ATP-dependent protease subunit HslV		RHIME		176	UniRef50_Q92TA9
ATP-dependent protease subunit HslV		SINFN		185
ATP-dependent protease subunit HslV		SINMW		185
ATP-dependent protease subunit HslV		MARMS		183
ATP-dependent protease subunit HslV		EHRRG		189
+1928

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L19201 Genomic DNA Translation: AAB03064.1 U00096 Genomic DNA Translation: AAC76914.1 AP009048 Genomic DNA Translation: BAE77378.1 D89965 mRNA Translation: BAA14040.1 Sequence problems. L14281 Genomic DNA No translation available.
PIRⁱ	JT0760
RefSeqⁱ	NP_418367.1, NC_000913.3 WP_000208242.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1E94	X-ray	2.80	A/B/C/D	2-176	[»]
	1G4A	X-ray	3.00	A/B/C/D	2-176	[»]
	1G4B	X-ray	7.00	M/N/O/P	2-176	[»]
	1HQY	X-ray	2.80	A/B/C/D	2-176	[»]
	1HT1	X-ray	2.80	A/B/C/D/V/X/Y/Z	2-176	[»]
	1HT2	X-ray	2.80	A/B/C/D/I/J/K/L	2-176	[»]
	1NED	X-ray	3.80	A/B/C	2-176	[»]
	4G4E	X-ray	2.89	A/B/C/D/E/F/G/H/I/J/K/L	2-175	[»]
	5JI3	X-ray	3.00	A/B/C/D	1-176	[»]
ProteinModelPortalⁱ	P0A7B8
SMRⁱ	P0A7B8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261781, 287 interactors
ComplexPortalⁱ	CPX-2104 HslUV protease complex
DIPⁱ	DIP-35866N
IntActⁱ	P0A7B8, 33 interactors
STRINGⁱ	316385.ECDH10B_4121

2D gel databases

SWISS-2DPAGEⁱ	P0A7B8

SWISS-2DPAGEⁱ

P0A7B8

Proteomic databases

EPDⁱ	P0A7B8
PaxDbⁱ	P0A7B8
PRIDEⁱ	P0A7B8

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76914; AAC76914; b3932 BAE77378; BAE77378; BAE77378
GeneIDⁱ	948429
KEGGⁱ	ecj:JW3903 eco:b3932
PATRICⁱ	fig\|1411691.4.peg.2773

Organism-specific databases

EchoBASEⁱ	EB1627
EcoGeneⁱ	EG11676 hslV

Phylogenomic databases

eggNOGⁱ	ENOG4108R5P Bacteria COG5405 LUCA
HOGENOMⁱ	HOG000064533
InParanoidⁱ	P0A7B8
KOⁱ	K01419
PhylomeDBⁱ	P0A7B8

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11676-MONOMER MetaCyc:EG11676-MONOMER
BRENDAⁱ	3.4.25.2 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P0A7B8
Protein Ontology More...PROⁱ	PR:P0A7B8

Family and domain databases

CDDⁱ	cd01913 protease_HslV, 1 hit
Gene3Dⁱ	3.60.20.10, 1 hit
HAMAPⁱ	MF_00248 HslV, 1 hit
InterProⁱ	View protein in InterPro IPR022281 ATP-dep_Prtase_HsIV_su IPR029055 Ntn_hydrolases_N IPR001353 Proteasome_sua/b IPR023333 Proteasome_suB-type
PANTHERⁱ	PTHR32194 PTHR32194, 1 hit
Pfamⁱ	View protein in Pfam PF00227 Proteasome, 1 hit
PIRSFⁱ	PIRSF039093 HslV, 1 hit
SUPFAMⁱ	SSF56235 SSF56235, 1 hit
TIGRFAMsⁱ	TIGR03692 ATP_dep_HslV, 1 hit
PROSITEⁱ	View protein in PROSITE PS51476 PROTEASOME_BETA_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HSLV_ECOLI
Accessionⁱ	P0A7B8Primary (citable) accession number: P0A7B8 Secondary accession number(s): P31059, P97542, Q2M8M8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 122 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Peptidase families
Classification of peptidase families and list of entries
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P0A7B8 (HSLV_ECOLI)

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ATP-dependent protease subunit HslV

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Temperature dependencei

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

Temperature dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ