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Protein

Chaperone protein ClpB 2

Gene

clpB2

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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 bindingi210 – 217ATP 1By similarity8
Nucleotide bindingi617 – 624ATP 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

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_0637-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein ClpB 2
Gene namesi
Name:clpB2
Ordered Locus Names:Synpcc7942_0637
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000002717 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001911891 – 895Chaperone protein ClpB 2Add BLAST895

Proteomic databases

PRIDEiO34209.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi1140.Synpcc7942_0637.

Structurei

3D structure databases

ProteinModelPortaliO34209.
SMRiO34209.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 145N-terminalBy similarityAdd BLAST145
Regioni163 – 346NBD1By similarityAdd BLAST184
Regioni347 – 557LinkerBy similarityAdd BLAST211
Regioni567 – 778NBD2By similarityAdd BLAST212
Regioni779 – 895C-terminalBy similarityAdd BLAST117

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili397 – 533By similarityAdd BLAST137

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

Phylogenomic databases

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
KOiK03695.
OrthoDBiPOG091H019M.

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.

O34209-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPTDPNRFT DQAWDAIVES QTVARQLRQQ QLEVEHVLLA LLDQESGVAA
60 70 80 90 100
EILAKAGVAV ANLRQPLEDF ARRQPRNASG TQLYLGRGLD RLLDLAERAR
110 120 130 140 150
ELWQDEFIGV EHLLMGFVED DRIGRRLAQG LKLDAKTLET TIQALRSPAA
160 170 180 190 200
DEAEAEESEP SYPFLSKYGR DLTALAEQEK LDPVIGRDLE IRRVIQVLSR
210 220 230 240 250
RSKNNPVLIG EPGVGKTAIA EGLAQRIVAG EVPDSLKQRR LISLDMGSLI
260 270 280 290 300
AGAKYRGEFE ERLRAVLHEV THSDGQMVLF IDELHTVVGA GAGQQGSAMD
310 320 330 340 350
AGNLLKPMLA RGELRCIGAT TTDEYRRTIE KDPALERRFQ QVYVSQPSVE
360 370 380 390 400
DTIAILRGLK ERYEGHHGVK ITDGALMAAA KLSHRYISDR FLPDKAIDLI
410 420 430 440 450
DEASAQLKME ITSKPSELED LERRLLQLEM EQLSLSGENG QASVHSDRLQ
460 470 480 490 500
QIQTELQTLQ EQQARLNQQW QQEKQLLEEL GRLQEEEETL RQQVNQAERE
510 520 530 540 550
HDLNKGAELK FGQLEALQQQ RQAIEEQIQA LHANGQTLLR EQVEEADIAE
560 570 580 590 600
IVARWTNIPV QRLLESERQK LLQLESFLHQ RVIGQDEAVV AVAAAIRRAR
610 620 630 640 650
AGMKDPSRPI GSFLFLGPTG VGKTELARAL ANCLFDAEDA LIRFDMSEYM
660 670 680 690 700
EKNSISRLIG APPGYIGYEE GGQLSEAIRR HPYAVVLFDE VEKAHPDVFN
710 720 730 740 750
LLLQVLDDGR ITDSQGRTID FCNAVIVMTS NIGSQFILEM GEEEASLDAV
760 770 780 790 800
ELKVLGALRQ HFRPEFLNRI DDTILFQPLS RGQLQQIVDI QLQRLKRLLA
810 820 830 840 850
EQAIALNVTP AAAANLADRG YDPVYGARPL KRAIQRLIEN PVASLILEQQ
860 870 880 890
FDAGDALIVD VDAEGQLQFQ VSKPVTATVV EPDDSPAIAV EAIPS
Length:895
Mass (Da):99,821
Last modified:January 1, 1998 - v1
Checksum:iEF5B0103EB513302
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97124 Genomic DNA. Translation: AAB72154.1.
CP000100 Genomic DNA. Translation: ABB56669.1.
RefSeqiWP_011243200.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB56669; ABB56669; Synpcc7942_0637.
KEGGisyf:Synpcc7942_0637.
PATRICi23786419. VBISynElo51371_0746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97124 Genomic DNA. Translation: AAB72154.1.
CP000100 Genomic DNA. Translation: ABB56669.1.
RefSeqiWP_011243200.1. NC_007604.1.

3D structure databases

ProteinModelPortaliO34209.
SMRiO34209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1140.Synpcc7942_0637.

Proteomic databases

PRIDEiO34209.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB56669; ABB56669; Synpcc7942_0637.
KEGGisyf:Synpcc7942_0637.
PATRICi23786419. VBISynElo51371_0746.

Phylogenomic databases

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
KOiK03695.
OrthoDBiPOG091H019M.

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_0637-MONOMER.

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 nameiCLPB2_SYNE7
AccessioniPrimary (citable) accession number: O34209
Secondary accession number(s): Q31QK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Not induced by heat shock or other stresses, it is expressed constitutively in the cell.

Keywords - Technical termi

Complete proteome, Reference proteome

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.