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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)DescriptionActionsGraphical viewLength
Active sitei6By similarity1
Metal bindingi161Sodium; via carbonyl oxygen1 Publication1
Metal bindingi164Sodium; via carbonyl oxygen1 Publication1
Metal bindingi167Sodium; via carbonyl oxygen1 Publication1

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_00003956181 – 5Removed in mature formCurated5
ChainiPRO_00001481546 – 176ATP-dependent protease subunit HslVAdd BLAST171

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

1176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 13Combined sources6
Beta strandi16 – 21Combined sources6
Beta strandi25 – 27Combined sources3
Beta strandi30 – 34Combined sources5
Beta strandi39 – 42Combined sources4
Turni43 – 46Combined sources4
Beta strandi47 – 53Combined sources7
Helixi55 – 71Combined sources17
Turni72 – 74Combined sources3
Helixi76 – 89Combined sources14
Helixi93 – 95Combined sources3
Beta strandi99 – 103Combined sources5
Beta strandi108 – 111Combined sources4
Beta strandi121 – 128Combined sources8
Helixi131 – 144Combined sources14
Helixi149 – 163Combined sources15
Beta strandi172 – 175Combined sources4

3D structure databases

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

Family and domain databases

CDDicd01913. protease_HslV. 1 hit.
Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00248. HslV. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M4YX-ray2.10A/B/C6-176[»]
ProteinModelPortaliQ9WYZ1.
SMRiQ9WYZ1.
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.

Miscellaneous databases

EvolutionaryTraceiQ9WYZ1.

Family and domain databases

CDDicd01913. protease_HslV. 1 hit.
Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00248. HslV. 1 hit.
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...

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: November 2, 2016
This is version 119 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.