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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Leptolyngbya boryana (Plectonema boryanum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi209 – 216ATP 1By similarity8
Nucleotide bindingi612 – 619ATP 2By similarity8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein ClpB
Gene namesi
Name:clpB
OrganismiLeptolyngbya boryana (Plectonema boryanum)
Taxonomic identifieri1184 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesLeptolyngbyaceaeLeptolyngbya

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001911551 – 873Chaperone protein ClpBAdd BLAST873

Proteomic databases

PRIDEiO87444.

Expressioni

Inductioni

By stress conditions, such as excess light and low temperatures.1 Publication

Interactioni

Subunit structurei

Homohexamer. The oligomerization is ATP-dependent (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO87444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 146N-terminalBy similarityAdd BLAST146
Regioni162 – 343NBD1By similarityAdd BLAST182
Regioni344 – 552LinkerBy similarityAdd BLAST209
Regioni562 – 773NBD2By similarityAdd BLAST212
Regioni774 – 873C-terminalBy similarityAdd BLAST100

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili394 – 528By similarityAdd BLAST135

Domaini

The N-terminal 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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the ClpA/ClpB family.Curated

Keywords - Domaini

Coiled coil, Repeat

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR017730. Chaperonin_ClpB.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF81923. SSF81923. 1 hit.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O87444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPTNSEKFT EKVWEAIYRT QEMYKQAQQQ QIETEHLMKA LLEQDGLAIS
60 70 80 90 100
IFNKLAVPVD RVRDRTDDFI RRQPKVSGSG TSVYWGRRAD ALLXRAEEYR
110 120 130 140 150
KQFEDSFISI EHLLLGYAQD SRFGKALLSE FRYPDEAKLR NAIEQVRGNQ
160 170 180 190 200
KVTDQTPENK YESLEKYGRD LTQYAREGKL DPVIGRDDEI RRTIQILSRR
210 220 230 240 250
TKNNPVLIGE PGVGKTAIAE GLAQRILSGD VPQSLKDRKL IALDMGALIA
260 270 280 290 300
GAKYRGEFEE RLKAVLKEVT DSRGNIILFI DEIHTVVGAG ATQGAMDAGN
310 320 330 340 350
LLKPMLARGE LRCIGATTLD EYRKYIEKDA ALERRFQQVF VDQPSVEDTI
360 370 380 390 400
SILRGLKERY EVHHGVKISD SALVAAATLS TRYISDRFLP SKAIDLVDEA
410 420 430 440 450
AAKLKMEITS KPEELDEVDR KVLQLEMERL SLQKENDAGS RDRLERLERE
460 470 480 490 500
LADFKEDQSK LNAQWQAEKS VITDLQKLKE EIDRVNLEIQ QAERDYDLNR
510 520 530 540 550
AAELKYGKLN ELNRKVEETE SQLSQIQKSG ATLLREEVLE SDIAEIISKW
560 570 580 590 600
TGIPVSKLVE SEMQKLLQLD DVLHQRVIGQ DEAVTAVSDA IQRSRAGLSD
610 620 630 640 650
PNRPTASFIF LGPTGVGKTE LAKALAAFLF DTEEAMVRID MSEYMEKHSV
660 670 680 690 700
SRLIGAPPGY VGYEEGGQLT EAVRRRPYSV ILFDEIEKAH PDVFNVMLQI
710 720 730 740 750
LDDGRVTDSQ GRTVDFKNTI IIMTSNIGSQ YIFEYGGDDD RYEEILSRVM
760 770 780 790 800
EAMLSNFRPE FLNRIDEIII FHSLQKAQLR EIVKIQTHRL ESRLARKMSL
810 820 830 840 850
KLSDAALDFL AEGFDPVYGA RPLKRAIQRE LETTIAKEIL RSNFTEGDTI
860 870
FVDVGETERL EFKRLPSEVL TTQ
Length:873
Mass (Da):99,305
Last modified:October 11, 2004 - v2
Checksum:iCDA07B752CCAE3B2
GO

Sequence cautioni

The sequence AAC62621 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061279 Genomic DNA. Translation: AAC62621.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061279 Genomic DNA. Translation: AAC62621.1. Different initiation.

3D structure databases

ProteinModelPortaliO87444.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO87444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR017730. Chaperonin_ClpB.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF81923. SSF81923. 1 hit.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCLPB_LEPBY
AccessioniPrimary (citable) accession number: O87444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.