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Protein

ATP-dependent protease subunit ClpQ

Gene

clpQ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease subunit of a proteasome-like degradation complex.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21
Metal bindingi165 – 1651Sodium; via carbonyl oxygen
Metal bindingi168 – 1681Sodium; via carbonyl oxygen
Metal bindingi171 – 1711Sodium; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Metal-binding, Sodium

Enzyme and pathway databases

BioCyciBSUB:BSU16150-MONOMER.

Protein family/group databases

MEROPSiT01.007.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent protease subunit ClpQ (EC:3.4.21.-)
Gene namesi
Name:clpQ
Synonyms:codW, hslV
Ordered Locus Names:BSU16150
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21S → A or T: Complete loss of protease activity. 1 Publication
Mutagenesisi6 – 61A → G: No effect. 1 Publication
Mutagenesisi7 – 71T → A: Complete loss of protease activity. The mutant is only found as a monomer; when associated with A-8. 1 Publication
Mutagenesisi8 – 81T → A: Complete loss of protease activity. The mutant is only found as a monomer; when associated with A-7. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 181180ATP-dependent protease subunit ClpQPRO_0000026678Add
BLAST

Proteomic databases

PaxDbiP39070.

Interactioni

Subunit structurei

A double ring-shaped homohexamer of ClpQ is capped on each side by a ring-shaped ClpY homohexamer. The assembly of the ClpQ/ClpY complex is dependent on binding of ATP (By similarity).By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008896.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146Combined sources
Beta strandi17 – 226Combined sources
Beta strandi26 – 283Combined sources
Turni29 – 313Combined sources
Beta strandi32 – 365Combined sources
Beta strandi41 – 444Combined sources
Turni45 – 484Combined sources
Beta strandi49 – 535Combined sources
Helixi57 – 7317Combined sources
Turni74 – 763Combined sources
Helixi78 – 9114Combined sources
Helixi95 – 973Combined sources
Beta strandi102 – 1054Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi123 – 1308Combined sources
Helixi133 – 14715Combined sources
Helixi148 – 1503Combined sources
Helixi153 – 16715Combined sources
Beta strandi176 – 1805Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YYFX-ray4.16C/D1-181[»]
2Z3AX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L2-181[»]
2Z3BX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L2-181[»]
ProteinModelPortaliP39070.
SMRiP39070. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39070.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family. HslV subfamily.Curated

Phylogenomic databases

eggNOGiENOG4108R5P. Bacteria.
COG5405. LUCA.
HOGENOMiHOG000064533.
InParanoidiP39070.
KOiK01419.
OMAiIMKGNAR.
PhylomeDBiP39070.

Family and domain databases

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.

P39070-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFHATTIF AVQHKGRSAM SGDGQVTFGQ AVVMKHTARK VRKLFNGKVL
60 70 80 90 100
AGFAGSVADA FTLFEKFEAK LEEYNGNLKR AAVELAKEWR SDKVLRKLEA
110 120 130 140 150
MLIVMNQDTL LLVSGTGEVI EPDDGILAIG SGGNYALAAG RALKKHAGES
160 170 180
MSASEIARAA LETAGEICVY TNDQIILEEL E
Length:181
Mass (Da):19,478
Last modified:February 1, 1995 - v1
Checksum:i95DC72474A41A97D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 54Missing in CAA83919 (Ref. 2) Curated
Sequence conflicti60 – 601A → R in CAA83919 (Ref. 2) Curated
Sequence conflicti72 – 721E → K in CAA83919 (Ref. 2) Curated

Mass spectrometryi

Molecular mass is 19345.7 Da from positions 2 - 181. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13634 Genomic DNA. Translation: AAB03370.1.
Z33639 Genomic DNA. Translation: CAA83919.1.
AL009126 Genomic DNA. Translation: CAB13488.1.
PIRiS61494.
RefSeqiNP_389497.1. NC_000964.3.
WP_003238555.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13488; CAB13488; BSU16150.
GeneIDi11239476.
938111.
KEGGibsu:BSU16150.
PATRICi18975035. VBIBacSub10457_1709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13634 Genomic DNA. Translation: AAB03370.1.
Z33639 Genomic DNA. Translation: CAA83919.1.
AL009126 Genomic DNA. Translation: CAB13488.1.
PIRiS61494.
RefSeqiNP_389497.1. NC_000964.3.
WP_003238555.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YYFX-ray4.16C/D1-181[»]
2Z3AX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L2-181[»]
2Z3BX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L2-181[»]
ProteinModelPortaliP39070.
SMRiP39070. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008896.

Protein family/group databases

MEROPSiT01.007.

Proteomic databases

PaxDbiP39070.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13488; CAB13488; BSU16150.
GeneIDi11239476.
938111.
KEGGibsu:BSU16150.
PATRICi18975035. VBIBacSub10457_1709.

Phylogenomic databases

eggNOGiENOG4108R5P. Bacteria.
COG5405. LUCA.
HOGENOMiHOG000064533.
InParanoidiP39070.
KOiK01419.
OMAiIMKGNAR.
PhylomeDBiP39070.

Enzyme and pathway databases

BioCyciBSUB:BSU16150-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39070.

Family and domain databases

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 nameiCLPQ_BACSU
AccessioniPrimary (citable) accession number: P39070
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 123 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, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.