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Entry version 137 (23 Feb 2022)
Sequence version 2 (24 May 2005)
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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.

1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi198 – 205ATP 18
Nucleotide bindingi595 – 602ATP 28

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.4.10, 2305

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Chaperone protein ClpB
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:clpB
Ordered Locus Names:TTHA1487
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiThermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri300852 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000532 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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

Keywords - Cellular componenti

Cytoplasm

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi167G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-475. 1 Publication1
Mutagenesisi204 – 205KT → AA: Loss of ability to bind ATP. Residual ATPase activity. 1 Publication2
Mutagenesisi270D → N: No effect on ability to bind ATP. Decrease in ATPase activity. 1 Publication1
Mutagenesisi271E → Q: No effect on ability to bind ATP. Increase in ATPase activity. 1 Publication1
Mutagenesisi350V → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-467. 1 Publication1
Mutagenesisi353G → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-464. 1 Publication1
Mutagenesisi355R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-520. 1 Publication1
Mutagenesisi396L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. 1 Publication1
Mutagenesisi460L → A: Great decrease in chaperone activity. Retains ATPase activity and oligomerization. 1 Publication1
Mutagenesisi464R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-353. 1 Publication1
Mutagenesisi467Q → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-350. 1 Publication1
Mutagenesisi475R → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-167. 1 Publication1
Mutagenesisi520E → C: Great decrease in chaperone activity. Retains ATPase activity and oligomerization; when associated with C-355. 1 Publication1
Mutagenesisi601 – 602KT → AA: Loss of ability to bind ATP. Residual ATPase activity. 1 Publication2
Mutagenesisi667D → N: Decrease in ATPase activity. 1 Publication1
Mutagenesisi668E → Q: Decrease in ATPase activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04395, Phosphoaminophosphonic Acid-Adenylate Ester

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001911951 – 854Chaperone protein ClpBAdd BLAST854

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9RA63

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer. The oligomerization is ATP-dependent.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-41758N

Protein interaction database and analysis system

More...
IntActi
Q9RA63, 1 interactor

Molecular INTeraction database

More...
MINTi
Q9RA63

STRING: functional protein association networks

More...
STRINGi
300852.55772869

<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

1854
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9RA63

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9RA63

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 147Clp RPROSITE-ProRule annotationAdd BLAST145

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni6 – 71Repeat 1PROSITE-ProRule annotationAdd BLAST66
Regioni83 – 147Repeat 2PROSITE-ProRule annotationAdd BLAST65
Regioni151 – 331NBD1Add BLAST181
Regioni332 – 535LinkerAdd BLAST204
Regioni545 – 756NBD2Add BLAST212
Regioni757 – 854C-terminalAdd BLAST98

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili382 – 516Add BLAST135

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer.

<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

Belongs to the ClpA/ClpB family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0542, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_005070_4_0_0

Identification of Orthologs from Complete Genome Data

More...
OMAi
QDPKRPI

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9RA63

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1780.10, 1 hit
3.40.50.300, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR003959, ATPase_AAA_core
IPR017730, Chaperonin_ClpB
IPR019489, Clp_ATPase_C
IPR036628, Clp_N_dom_sf
IPR004176, Clp_R_dom
IPR001270, ClpA/B
IPR018368, ClpA/B_CS1
IPR028299, ClpA/B_CS2
IPR041546, ClpA/ClpB_AAA_lid
IPR027417, P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004, AAA, 1 hit
PF07724, AAA_2, 1 hit
PF17871, AAA_lid_9, 1 hit
PF02861, Clp_N, 2 hits
PF10431, ClpB_D2-small, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00300, CLPPROTEASEA

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 2 hits
SM01086, ClpB_D2-small, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 2 hits
SSF81923, SSF81923, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03346, chaperone_ClpB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51903, CLP_R, 1 hit
PS00870, CLPAB_1, 1 hit
PS00871, CLPAB_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9RA63-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLERWTQAA REALAQAQVL AQRMKHQAID LPHLWAVLLK DERSLAWRLL
60 70 80 90 100
EKAGADPKAL KELQERELAR LPKVEGAEVG QYLTSRLSGA LNRAEALMEE
110 120 130 140 150
LKDRYVAVDT LVLALAEATP GLPGLEALKG ALKELRGGRT VQTEHAESTY
160 170 180 190 200
NALEQYGIDL TRLAAEGKLD PVIGRDEEIR RVIQILLRRT KNNPVLIGEP
210 220 230 240 250
GVGKTAIVEG LAQRIVKGDV PEGLKGKRIV SLQMGSLLAG AKYRGEFEER
260 270 280 290 300
LKAVIQEVVQ SQGEVILFID ELHTVVGAGK AEGAVDAGNM LKPALARGEL
310 320 330 340 350
RLIGATTLDE YREIEKDPAL ERRFQPVYVD EPTVEETISI LRGLKEKYEV
360 370 380 390 400
HHGVRISDSA IIAAATLSHR YITERRLPDK AIDLIDEAAA RLRMALESAP
410 420 430 440 450
EEIDALERKK LQLEIEREAL KKEKDPDSQE RLKAIEAEIA KLTEEIAKLR
460 470 480 490 500
AEWEREREIL RKLREAQHRL DEVRREIELA ERQYDLNRAA ELRYGELPKL
510 520 530 540 550
EAEVEALSEK LRGARFVRLE VTEEDIAEIV SRWTGIPVSK LLEGEREKLL
560 570 580 590 600
RLEEELHKRV VGQDEAIRAV ADAIRRARAG LKDPNRPIGS FLFLGPTGVG
610 620 630 640 650
KTELAKTLAA TLFDTEEAMI RIDMTEYMEK HAVSRLIGAP PGYVGYEEGG
660 670 680 690 700
QLTEAVRRRP YSVILFDEIE KAHPDVFNIL LQILDDGRLT DSHGRTVDFR
710 720 730 740 750
NTVIILTSNL GSPLILEGLQ KGWPYERIRD EVFKVLQQHF RPEFLNRLDE
760 770 780 790 800
IVVFRPLTKE QIRQIVEIQL SYLRARLAEK RISLELTEAA KDFLAERGYD
810 820 830 840 850
PVFGARPLRR VIQRELETPL AQKILAGEVK EGDRVQVDVG PAGLVFAVPA

RVEA
Length:854
Mass (Da):96,254
Last modified:May 24, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFB9A39BB040363E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti96A → G in BAA81745 (PubMed:10377389).Curated1
Sequence conflicti96A → G in BAA96085 (PubMed:10377389).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB012390 Genomic DNA Translation: BAA81745.1
AB032368 Genomic DNA Translation: BAA96085.1
AP008226 Genomic DNA Translation: BAD71310.1
Y07826 Genomic DNA Translation: CAA69163.2

NCBI Reference Sequences

More...
RefSeqi
WP_011228712.1, NC_006461.1
YP_144753.1, NC_006461.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAD71310; BAD71310; BAD71310

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3167975

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ttj:TTHA1487

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|300852.9.peg.1462

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012390 Genomic DNA Translation: BAA81745.1
AB032368 Genomic DNA Translation: BAA96085.1
AP008226 Genomic DNA Translation: BAD71310.1
Y07826 Genomic DNA Translation: CAA69163.2
RefSeqiWP_011228712.1, NC_006461.1
YP_144753.1, NC_006461.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
1QVRX-ray3.00A/B/C1-854[»]
4FCTX-ray4.00A545-852[»]
4FCVX-ray3.40A/B/C544-852[»]
4FCWX-ray2.35A/C/F544-852[»]
4FD2X-ray3.00A/B/D545-852[»]
4HSEX-ray2.20A142-534[»]
4LJ4X-ray2.80A520-854[»]
4LJ5X-ray2.40A520-854[»]
4LJ6X-ray1.90A520-854[»]
4LJ7X-ray2.80A/B/C520-854[»]
4LJ8X-ray2.10A520-854[»]
4LJ9X-ray1.70A520-854[»]
4LJAX-ray2.00A520-854[»]
SMRiQ9RA63
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-41758N
IntActiQ9RA63, 1 interactor
MINTiQ9RA63
STRINGi300852.55772869

Chemistry databases

DrugBankiDB04395, Phosphoaminophosphonic Acid-Adenylate Ester

Proteomic databases

PRIDEiQ9RA63

Genome annotation databases

EnsemblBacteriaiBAD71310; BAD71310; BAD71310
GeneIDi3167975
KEGGittj:TTHA1487
PATRICifig|300852.9.peg.1462

Phylogenomic databases

eggNOGiCOG0542, Bacteria
HOGENOMiCLU_005070_4_0_0
OMAiQDPKRPI
PhylomeDBiQ9RA63

Enzyme and pathway databases

BRENDAi3.6.4.10, 2305

Miscellaneous databases

EvolutionaryTraceiQ9RA63

Family and domain databases

Gene3Di1.10.1780.10, 1 hit
3.40.50.300, 3 hits
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR003959, ATPase_AAA_core
IPR017730, Chaperonin_ClpB
IPR019489, Clp_ATPase_C
IPR036628, Clp_N_dom_sf
IPR004176, Clp_R_dom
IPR001270, ClpA/B
IPR018368, ClpA/B_CS1
IPR028299, ClpA/B_CS2
IPR041546, ClpA/ClpB_AAA_lid
IPR027417, P-loop_NTPase
PfamiView protein in Pfam
PF00004, AAA, 1 hit
PF07724, AAA_2, 1 hit
PF17871, AAA_lid_9, 1 hit
PF02861, Clp_N, 2 hits
PF10431, ClpB_D2-small, 1 hit
PRINTSiPR00300, CLPPROTEASEA
SMARTiView protein in SMART
SM00382, AAA, 2 hits
SM01086, ClpB_D2-small, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
SSF81923, SSF81923, 1 hit
TIGRFAMsiTIGR03346, chaperone_ClpB, 1 hit
PROSITEiView protein in PROSITE
PS51903, CLP_R, 1 hit
PS00870, CLPAB_1, 1 hit
PS00871, CLPAB_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCLPB_THET8
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9RA63
Secondary accession number(s): P74942, Q5SI87
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 24, 2005
Last modified: February 23, 2022
This is version 137 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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