Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O34209

- CLPB2_SYNE7

UniProt

O34209 - CLPB2_SYNE7

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Chaperone protein ClpB 2

Gene

clpB2

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi210 – 2178ATP 1By similarity
Nucleotide bindingi617 – 6248ATP 2By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. protein processing Source: InterPro
  2. response to heat Source: InterPro
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 lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002717: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 895895Chaperone protein ClpB 2PRO_0000191189Add
BLAST

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. Positions 165-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 145145N-terminalBy similarityAdd
BLAST
Regioni163 – 346184NBD1By similarityAdd
BLAST
Regioni347 – 557211LinkerBy similarityAdd
BLAST
Regioni567 – 778212NBD2By similarityAdd
BLAST
Regioni779 – 895117C-terminalBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili397 – 533137By similarityAdd
BLAST

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

eggNOGiCOG0542.
HOGENOMiHOG000218211.
KOiK03695.
OrthoDBiEOG65F8SM.

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.
IPR023150. Dbl_Clp-N.
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.
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:
EMBL
GenBank
DDBJ
Links Updated
U97124 Genomic DNA. Translation: AAB72154.1.
CP000100 Genomic DNA. Translation: ABB56669.1.
RefSeqiYP_399656.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB56669; ABB56669; Synpcc7942_0637.
GeneIDi3775620.
KEGGisyf:Synpcc7942_0637.
PATRICi23786419. VBISynElo51371_0746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U97124 Genomic DNA. Translation: AAB72154.1 .
CP000100 Genomic DNA. Translation: ABB56669.1 .
RefSeqi YP_399656.1. NC_007604.1.

3D structure databases

ProteinModelPortali O34209.
SMRi O34209. Positions 165-357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 1140.Synpcc7942_0637.

Proteomic databases

PRIDEi O34209.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB56669 ; ABB56669 ; Synpcc7942_0637 .
GeneIDi 3775620.
KEGGi syf:Synpcc7942_0637.
PATRICi 23786419. VBISynElo51371_0746.

Phylogenomic databases

eggNOGi COG0542.
HOGENOMi HOG000218211.
KOi K03695.
OrthoDBi EOG65F8SM.

Enzyme and pathway databases

BioCyci SYNEL:SYNPCC7942_0637-MONOMER.

Family and domain databases

Gene3Di 1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. 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.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view ]
PRINTSi PR00300. CLPPROTEASEA.
SMARTi SM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
TIGRFAMsi TIGR03346. chaperone_ClpB. 1 hit.
PROSITEi PS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus."
    Eriksson M.J., Schelin J., Miskiewicz E., Clarke A.K.
    J. Bacteriol. 183:7392-7396(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.

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: October 29, 2014
This is version 88 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

External Data

Dasty 3