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Entry version 140 (11 Dec 2019)
Sequence version 1 (11 Oct 2004)
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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Escherichia coli (strain K12)
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.3 Publications

Miscellaneous

One peptide binds per ClpB hexamer; the binding site is formed only upon ATP-driven oligomerization.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi206 – 213ATP 18
Nucleotide bindingi605 – 612ATP 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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10157-MONOMER
ECOL316407:JW2573-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P63284

<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_and_taxonomy_section">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
Alternative name(s):
Heat shock protein F84.1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
Synonyms:htpM
Ordered Locus Names:b2592, JW2573
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
  • UP000000625 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

GO - Cellular componenti

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_and_biotech_section">'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>Mutagenesisi7T → A: Loss of chaperone activity. 1 Publication1
Mutagenesisi84S → A: No effect. 1 Publication1
Mutagenesisi93L → Q: Loss of chaperone activity. Retains ATPase activity. 1 Publication1
Mutagenesisi97L → Q: 75% decrease in chaperone activity; retains ATPase activity. 1 Publication1
Mutagenesisi103D → A: Loss of chaperone activity. 1 Publication1
Mutagenesisi109E → A: Loss of chaperone activity. 1 Publication1
Mutagenesisi110L → Q: 30% decrease in chaperone activity; retains ATPase activity. 1 Publication1
Mutagenesisi212K → T: Loss of ability to form oligomers even in the presence of ATP. Loss of chaperone activity. 3 Publications1
Mutagenesisi251Y → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity. 1 Publication1
Mutagenesisi254E → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity; when associated with A-257. 1 Publication1
Mutagenesisi257E → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity; when associated with A-254. 1 Publication1
Mutagenesisi279E → A: No effect on oligomerization. 1 Publication1
Mutagenesisi332R → A: Loss of ability to form oligomers. 1 Publication1
Mutagenesisi543W → F: No effect on chaperone activity or ability to form oligomers. 1 Publication1
Mutagenesisi611K → T: No effect on ability to form oligomers. Loss of chaperone activity. 3 Publications1
Mutagenesisi678E → A: No effect on oligomerization. 1 Publication1
Mutagenesisi756R → A: No effect on oligomerization. Loss of ATPase activity. 1 Publication1
Mutagenesisi797D → A: No effect. 1 Publication1
Mutagenesisi813 – 815GAR → AAA: No effect on oligomerization. 1 Publication3
Mutagenesisi815R → A: Loss of ability to form oligomers; loss of chaperone activity. 1 Publication1
Mutagenesisi819R → A: Loss of ability to form oligomers; loss of chaperone activity. 1 Publication1
Mutagenesisi826E → A: No effect. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000054911 – 857Chaperone protein ClpBAdd BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei96N6-acetyllysine1 Publication1
Modified residuei176N6-acetyllysine1 Publication1
Modified residuei640N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P63284

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P63284

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P63284

PRoteomics IDEntifications database

More...
PRIDEi
P63284

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P63284

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P63284

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P63284

<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 subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By heat shock and other environmental stresses.

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer. The oligomerization is ATP-dependent.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260618, 221 interactors
851414, 32 interactors

Database of interacting proteins

More...
DIPi
DIP-35844N

Protein interaction database and analysis system

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IntActi
P63284, 81 interactors

Molecular INTeraction database

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MINTi
P63284

STRING: functional protein association networks

More...
STRINGi
511145.b2592

<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

1857
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

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SMRi
P63284

Database of comparative protein structure models

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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
P63284

<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_and_domains_section">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 – 146Clp RPROSITE-ProRule annotationAdd BLAST144

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 – 146Repeat 2PROSITE-ProRule annotationAdd BLAST64
Regioni159 – 340NBD1Add BLAST182
Regioni341 – 545LinkerAdd BLAST205
Regioni555 – 765NBD2Add BLAST211
Regioni766 – 857C-terminalAdd BLAST92

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 coili391 – 525By similarityAdd 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
ENOG4105C2Z Bacteria
COG0542 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000218211

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P63284

KEGG Orthology (KO)

More...
KOi
K03695

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P63284

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1780.10, 1 hit

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
IPR004176 Clp_N
IPR036628 Clp_N_dom_sf
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_length">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>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform ClpB (identifier: P63284-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL
60 70 80 90 100
TSAGINAGQL RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK
110 120 130 140 150
RGDNFISSEL FVLAALESRG TLADILKAAG ATTANITQAI EQMRGGESVN
160 170 180 190 200
DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV IGRDEEIRRT IQVLQRRTKN
210 220 230 240 250
NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL DMGALVAGAK
260 270 280 290 300
YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
310 320 330 340 350
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL
360 370 380 390 400
RGLKERYELH HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS
410 420 430 440 450
IRMQIDSKPE ELDRLDRRII QLKLEQQALM KESDEASKKR LDMLNEELSD
460 470 480 490 500
KERQYSELEE EWKAEKASLS GTQTIKAELE QAKIAIEQAR RVGDLARMSE
510 520 530 540 550
LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL ARWTGIPVSR
560 570 580 590 600
MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS
610 620 630 640 650
FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP
660 670 680 690 700
PGYVGYEEGG YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT
710 720 730 740 750
DGQGRTVDFR NTVVIMTSNL GSDLIQERFG ELDYAHMKEL VLGVVSHNFR
760 770 780 790 800
PEFINRIDEV VVFHPLGEQH IASIAQIQLK RLYKRLEERG YEIHISDEAL
810 820 830 840 850
KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP GKVIRLEVNE

DRIVAVQ
Length:857
Mass (Da):95,585
Last modified:October 11, 2004 - v1
<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:iFD38CD96B2F7C32A
GO
Isoform ClpB-3 (identifier: P63284-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
     149-149: V → M

Note: ClpB-3 ATPase activity is not activated by proteins, as it is in ClpB.Curated
Show »
Length:709
Mass (Da):79,870
Checksum:i60270862D6198B55
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 conflicti96 – 97KL → NV in AAA24422 (PubMed:2185473).Curated2
Sequence conflicti122L → V in AAA24422 (PubMed:2185473).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0187031 – 148Missing in isoform ClpB-3. CuratedAdd BLAST148
Alternative sequenceiVSP_018987149V → M in isoform ClpB-3. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M29364 Genomic DNA Translation: AAA24422.1
U00096 Genomic DNA Translation: AAC75641.1
AP009048 Genomic DNA Translation: BAA16476.1
X57620 Genomic DNA Translation: CAA40846.1
V00350 Genomic DNA Translation: CAA23639.1
U50134 Genomic DNA Translation: AAA92959.1

Protein sequence database of the Protein Information Resource

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PIRi
C65037 D35905

NCBI Reference Sequences

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RefSeqi
NP_417083.1, NC_000913.3
WP_001235102.1, NZ_STEB01000040.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75641; AAC75641; b2592
BAA16476; BAA16476; BAA16476

Database of genes from NCBI RefSeq genomes

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GeneIDi
947077

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW2573
eco:b2592

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4145

Keywords - Coding sequence diversityi

Alternative initiation

<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
M29364 Genomic DNA Translation: AAA24422.1
U00096 Genomic DNA Translation: AAC75641.1
AP009048 Genomic DNA Translation: BAA16476.1
X57620 Genomic DNA Translation: CAA40846.1
V00350 Genomic DNA Translation: CAA23639.1
U50134 Genomic DNA Translation: AAA92959.1
PIRiC65037 D35905
RefSeqiNP_417083.1, NC_000913.3
WP_001235102.1, NZ_STEB01000040.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JBKX-ray1.80A159-351[»]
1KHYX-ray1.95A/B/C/D1-148[»]
4CIUX-ray3.50A143-857[»]
4D2Qelectron microscopy18.00A/B/C/D/E/F1-857[»]
4D2Uelectron microscopy17.00A/B/C/D/E/F1-857[»]
4D2Xelectron microscopy20.00A/B/C/D/E/F1-857[»]
5OFOelectron microscopy4.60A/B/C/D/E/F1-721[»]
A/B/C/D/E/F750-857[»]
5OG1electron microscopy4.50A/B/C/D/E/F1-721[»]
A/B/C/D/E/F750-857[»]
6OG3electron microscopy4.10A/C/E1-857[»]
6QS6electron microscopy3.90A/B/C/D/E/F1-857[»]
6QS7electron microscopy3.80A/B/C/D/E/F1-857[»]
6QS8electron microscopy3.90A/B/C/D/E/F1-857[»]
SMRiP63284
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4260618, 221 interactors
851414, 32 interactors
DIPiDIP-35844N
IntActiP63284, 81 interactors
MINTiP63284
STRINGi511145.b2592

PTM databases

CarbonylDBiP63284
iPTMnetiP63284

2D gel databases

SWISS-2DPAGEiP63284

Proteomic databases

EPDiP63284
jPOSTiP63284
PaxDbiP63284
PRIDEiP63284

Genome annotation databases

EnsemblBacteriaiAAC75641; AAC75641; b2592
BAA16476; BAA16476; BAA16476
GeneIDi947077
KEGGiecj:JW2573
eco:b2592
PATRICifig|1411691.4.peg.4145

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB0155

Phylogenomic databases

eggNOGiENOG4105C2Z Bacteria
COG0542 LUCA
HOGENOMiHOG000218211
InParanoidiP63284
KOiK03695
PhylomeDBiP63284

Enzyme and pathway databases

BioCyciEcoCyc:EG10157-MONOMER
ECOL316407:JW2573-MONOMER
SABIO-RKiP63284

Miscellaneous databases

EvolutionaryTraceiP63284

Protein Ontology

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PROi
PR:P63284

Family and domain databases

Gene3Di1.10.1780.10, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR017730 Chaperonin_ClpB
IPR019489 Clp_ATPase_C
IPR004176 Clp_N
IPR036628 Clp_N_dom_sf
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_ECOLI
<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: P63284
Secondary accession number(s): P03815
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 11, 2004
Last modified: December 11, 2019
This is version 140 of the entry and version 1 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, Direct protein sequencing, 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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