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Protein

ATP-dependent protease subunit HslV

Gene

hslV

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.1 Publication

Catalytic activityi

ATP-dependent cleavage of peptide bonds with broad specificity.1 Publication

Enzyme regulationi

Allosterically activated by HslU binding.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei6 – 61By similarity
Metal bindingi161 – 1611Sodium; via carbonyl oxygen1 Publication
Metal bindingi164 – 1641Sodium; via carbonyl oxygen1 Publication
Metal bindingi167 – 1671Sodium; via carbonyl oxygen1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Ligandi

Metal-binding, Sodium

Protein family/group databases

MEROPSiT01.006.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent protease subunit HslV (EC:3.4.25.2)
Gene namesi
Name:hslV
Ordered Locus Names:TM_0521
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 55Removed in mature formCuratedPRO_0000395618
Chaini6 – 176171ATP-dependent protease subunit HslVPRO_0000148154Add
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.1 Publication

Protein-protein interaction databases

STRINGi243274.TM0521.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 136Combined sources
Beta strandi16 – 216Combined sources
Beta strandi25 – 273Combined sources
Beta strandi30 – 345Combined sources
Beta strandi39 – 424Combined sources
Turni43 – 464Combined sources
Beta strandi47 – 537Combined sources
Helixi55 – 7117Combined sources
Turni72 – 743Combined sources
Helixi76 – 8914Combined sources
Helixi93 – 953Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi121 – 1288Combined sources
Helixi131 – 14414Combined sources
Helixi149 – 16315Combined sources
Beta strandi172 – 1754Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M4YX-ray2.10A/B/C6-176[»]
ProteinModelPortaliQ9WYZ1.
SMRiQ9WYZ1. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WYZ1.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family. HslV subfamily.Curated

Phylogenomic databases

eggNOGiENOG4108R5P. Bacteria.
COG5405. LUCA.
InParanoidiQ9WYZ1.
KOiK01419.
OMAiIMKGNAR.
OrthoDBiEOG6ND0PJ.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00248. HslV.
InterProiIPR022281. ATP-dep_Prtase_HsIV_su.
IPR029055. Ntn_hydrolases_N.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF039093. HslV. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03692. ATP_dep_HslV. 1 hit.
PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9WYZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFHGTTILV VRRNGQTVMG GDGQVTFGST VLKGNARKVR KLGEGKVLAG
60 70 80 90 100
FAGSVADAMT LFDRFEAKLR EWGGNLTKAA VELAKDWRTD RVLRRLEALL
110 120 130 140 150
LVADKENIFI ISGNGEVIQP DDDAAAIGSG GPYALAAAKA LLRNTDLSAR
160 170
EIVEKAMTIA GEICIYTNQN IVIEEV
Length:176
Mass (Da):18,933
Last modified:November 1, 1999 - v1
Checksum:iECE369602A0ABD02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35606.1.
PIRiG72365.
RefSeqiNP_228331.1. NC_000853.1.
WP_004081403.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35606; AAD35606; TM_0521.
GeneIDi897572.
KEGGitma:TM0521.
PATRICi23935947. VBITheMar51294_0528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35606.1.
PIRiG72365.
RefSeqiNP_228331.1. NC_000853.1.
WP_004081403.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M4YX-ray2.10A/B/C6-176[»]
ProteinModelPortaliQ9WYZ1.
SMRiQ9WYZ1. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0521.

Protein family/group databases

MEROPSiT01.006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35606; AAD35606; TM_0521.
GeneIDi897572.
KEGGitma:TM0521.
PATRICi23935947. VBITheMar51294_0528.

Phylogenomic databases

eggNOGiENOG4108R5P. Bacteria.
COG5405. LUCA.
InParanoidiQ9WYZ1.
KOiK01419.
OMAiIMKGNAR.
OrthoDBiEOG6ND0PJ.

Miscellaneous databases

EvolutionaryTraceiQ9WYZ1.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00248. HslV.
InterProiIPR022281. ATP-dep_Prtase_HsIV_su.
IPR029055. Ntn_hydrolases_N.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF039093. HslV. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03692. ATP_dep_HslV. 1 hit.
PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV."
    Song H.K., Bochtler M., Azim M.K., Hartmann C., Huber R., Ramachandran R.
    Biophys. Chem. 100:437-452(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 6-176 IN COMPLEX WITH SODIUM, FUNCTION, PROPEPTIDE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiHSLV_THEMA
AccessioniPrimary (citable) accession number: Q9WYZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: April 13, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

According to PubMed:12646382 the propeptide is autoprocessed in 20% of the cases in the expression system (E.coli).

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  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.