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P74459 (CLPB1_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chaperone protein ClpB 1
Gene names
Name:clpB1
Ordered Locus Names:slr0156
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Subunit structure

Homohexamer. The oligomerization is ATP-dependent By similarity.

Subcellular location

Cytoplasm Probable.

Domain

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.

Sequence similarities

Belongs to the clpA/clpB family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein processing

Inferred from electronic annotation. Source: InterPro

response to heat

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Chaperone protein ClpB 1
PRO_0000191192

Regions

Nucleotide binding208 – 2158ATP 1 By similarity
Nucleotide binding620 – 6278ATP 2 By similarity
Region1 – 145145N-terminal By similarity
Region161 – 344184NBD1 By similarity
Region345 – 560216Linker By similarity
Region570 – 781212NBD2 By similarity
Region782 – 898117C-terminal By similarity
Coiled coil395 – 536142 By similarity

Sequences

Sequence LengthMass (Da)Tools
P74459 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 67BBA62136E36D63

FASTA898101,392
        10         20         30         40         50         60 
MQPTDPTKFT EQAWDAIVKS QEVARRYKNT NLEVEHILLA LLEQDMGLAA RIFQRAAVDG 

        70         80         90        100        110        120 
EGLRQQLEIF TNRQPKQAYV EQLYLGRSLD VMLDRADAAR SSWEDKFISV EHLLVGFAED 

       130        140        150        160        170        180 
DRVGRKTLRA FNLDPQDLEL AIKAIRGSQK VTEPNQEEKY EALDKYGRDL TEQARQGKLD 

       190        200        210        220        230        240 
PVIGRDEEIR RVIQVLSRRS KNNPVLIGEP GVGKTAIAEG LAQRIINGDV PESLKNRQLI 

       250        260        270        280        290        300 
SLDMGSLIAG AKYRGEFEER LRSVMKEVTN SDGQIILFID EVHTVVGAGG REGSGSMDAG 

       310        320        330        340        350        360 
NLLKPMLARG ELRCIGATTL DEYRKNIEKD PALERRFQQV YVKQPSVDDT ISILRGLKEK 

       370        380        390        400        410        420 
YEVHHGVKIT DSALVAAATL SHRYIQDRFL PDKAIDLVDE AAARLKMEIT SKPVELEDID 

       430        440        450        460        470        480 
RRLMQLQMEK LSLEGEEKRP GLGADKSSKE RLEKIQQEIT ELEGQQQELS GQWLSEKQML 

       490        500        510        520        530        540 
EEINTLKEKE QELRLQVEKA ERATDWEKAA KIKYGELEVL QHDIEEKESK LLEIQGSGNT 

       550        560        570        580        590        600 
LLREQVTESD IAEIVAGWTG IPMNRLMETE RQKLLQLEGH LHQRVIGQKE AVAAVSAAIR 

       610        620        630        640        650        660 
RARAGMKDPS RPIGSFLFMG PTGVGKTELA RALAGFLFDS EEAMVRIDMS EYMEKHAVSR 

       670        680        690        700        710        720 
LIGAPPGYVG YEEGGQLSEA VRRRPYSVVL LDEVEKAHLD VFNILLQVLD DGRITDSQGR 

       730        740        750        760        770        780 
VVDFRNTIIV MTSNIGSDHI LSLSADDADY DKMQKQVLQS LRKHFRPEFL NRIDDLIIFH 

       790        800        810        820        830        840 
TLKRDELRRI VVLQIKRIEK LLDEQKITLS LSDAALDHIV SAGYDPTYGA RPLKRAIQRQ 

       850        860        870        880        890 
LENPIATKIL ENTFVAGDKI LIDCVDGQLI FDKEIEPTTL PEEPEENITA VEVEVLSS 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA18560.1.
PIRS76431.
RefSeqNP_441882.1. NC_000911.1.
YP_005651942.1. NC_017277.1.
YP_007451763.1. NC_020286.1.

3D structure databases

ProteinModelPortalP74459.
SMRP74459. Positions 161-355.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48813N.
IntActP74459. 2 interactions.
STRING1148.slr0156.

Proteomic databases

PaxDbP74459.
PRIDEP74459.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18560; BAA18560; BAA18560.
GeneID12254601.
14617430.
952862.
KEGGsyn:slr0156.
syy:SYNGTS_1989.
PATRIC23841298. VBISynSp132158_2199.

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
KOK03695.
OMASDQLYLG.
ProtClustDBCLSK893322.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR018368. Chaperonin_ClpA/B_CS.
IPR017730. Chaperonin_ClpB.
IPR001270. Chaprnin_ClpA/B.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR03346. chaperone_ClpB. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB1_SYNY3
AccessionPrimary (citable) accession number: P74459
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: February 1, 1997
Last modified: May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families