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Q7V2A3 (CLPB_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chaperone protein ClpB
Gene names
Name:clpB
Ordered Locus Names:PMM0580
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorales › Prochlorococcaceae › Prochlorococcus ›

Protein attributes

Sequence length860 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
Gene Ontology (GO)
   Biological_processprotein metabolic process

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 860860Chaperone protein ClpB
PRO_0000191160

Regions

Nucleotide binding204 – 2118ATP 1 By similarity
Nucleotide binding608 – 6158ATP 2 By similarity
Region1 – 142142N-terminal By similarity
Region157 – 338182NBD1 By similarity
Region339 – 548210Linker By similarity
Region558 – 769212NBD2 By similarity
Region770 – 86091C-terminal By similarity
Coiled coil389 – 523135 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V2A3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 57C75FFA3B960A1E

FASTA86097,364
        10         20         30         40         50         60 
MKFVPSEFSN SAWDIFILSK EIAQNNFQQN IDSENILLAL IKQDLLTSKI LKKNCVNIRK 

        70         80         90        100        110        120 
IETKLTSLLD AKAKMKNKQK TLFIGETTEK VFLKANDLRV SFNDVVISTE HILYGLSYDE 

       130        140        150        160        170        180 
ICSELVLNTK KIPEFLELLN KMKSESTIND NFESSNETLD KFGIDLTKSA RDGILDPVIG 

       190        200        210        220        230        240 
RDEEIRRTIQ ILSRRTKNNP VLIGEPGVGK TAIVEGLAQR IVNGDVPSSL NNRQLISIDM 

       250        260        270        280        290        300 
GSLIAGAKYR GEFEERIKNV LKKVKSSEGK IILFIDEIHT VVGAGATGGS LDASNLLKPM 

       310        320        330        340        350        360 
LARGELRCIG ATTINEHKQN IEKDPALERR FQKIKINAPS VDDTISILRG LREKYEVHHS 

       370        380        390        400        410        420 
VRISDNALVA AASLSERYIN DRFLPDKAID LIDEAASRLN MIITSKPEEI DEIDRKVLQL 

       430        440        450        460        470        480 
EMENLSLQRE SDNFSLERLK RINNELHDLK IRQSELNHQW QKEKEEIDEI SNLKEEIEST 

       490        500        510        520        530        540 
QLKIEQAKRS FDLNKAAELE FGTLISLQKK LKIKSENLVD SFKSGEKNLL RQEVNFDDIA 

       550        560        570        580        590        600 
EVVSKWTSIP VNNLNQSEKE KLLKLELTLK EKIIGQNNAI CAVSDSIKRS RTGLNDPNRP 

       610        620        630        640        650        660 
IASFLFLGPT GVGKTELSKV IAKTIFDSNS SITRLDMSEY MEKHSVSKII GAPPGYLGFE 

       670        680        690        700        710        720 
SGGQLTEAVR KNPYSLILLD EIEKAHKDVL DVLLQVLDDG IITDGQGRTI SFKNSIIVLT 

       730        740        750        760        770        780 
SNLGSQSIND LSIRNEDKNE IKNIVNVELK KFFKPEFLNR LDEIIIFQNL ELNELKDIAK 

       790        800        810        820        830        840 
LQLKKLENRL IKKDLNFQIT DEAIDHLVKN SFDNSYGARP LKRIIQKEIE TKIANNILNN 

       850        860 
NYLNKKEVYI SIKDGCIFVN

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References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX548174 Genomic DNA. Translation: CAE19039.1.
RefSeqNP_892698.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V2A3.
SMRQ7V2A3. Positions 157-349.
ModBaseSearch...

Protein-protein interaction databases

STRING59919.PMM0580.

Proteomic databases

PRIDEQ7V2A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE19039; CAE19039; PMM0580.
GeneID1726725.
KEGGpmm:PMM0580.
PATRIC23031932. VBIProMar68066_0635.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
KOK03695.
OMAANDHHED.
ProtClustDBCLSK921898.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-601-MONOMER.

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.
IPR001270. Chaprnin_ClpA/B.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR023150. Dbl_Clp-N.
[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]
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB_PROMP
AccessionPrimary (citable) accession number: Q7V2A3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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