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Q7V8B1 (CLPB_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. 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:PMT_0449
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorales › Prochlorococcaceae › Prochlorococcus ›

Protein attributes

Sequence length865 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 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 – 865865Chaperone protein ClpB
PRO_0000191159

Regions

Nucleotide binding207 – 2148ATP 1 By similarity
Nucleotide binding611 – 6188ATP 2 By similarity
Region1 – 144144N-terminal By similarity
Region160 – 341182NBD1 By similarity
Region342 – 551210Linker By similarity
Region561 – 772212NBD2 By similarity
Region773 – 86593C-terminal By similarity
Coiled coil392 – 526135 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V8B1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: E52459560CF5C260

FASTA86595,779
        10         20         30         40         50         60 
MQPTADQFTE KGWAAIVLAQ QLAQQRKHQQ LETEHLLLSL LQQNALAGRI LEKAGVSIGN 

        70         80         90        100        110        120 
LQTAVEAHLQ EQPTMQAAPD SVYLGKGVND LLDQAEKHKQ AFGDSFISIE HLLLALAGDN 

       130        140        150        160        170        180 
RCGRKLLNQA GVDAGKLKVA IDAVRGNQKV TDQNPEGTYE SLEKYGRDLS AAAREGKLDP 

       190        200        210        220        230        240 
VIGRDDEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP AALQNRQLIT 

       250        260        270        280        290        300 
LDMGALIAGA KYRGEFEERL KAVLKEVTAS EGQIVLFIDE IHTVVGAGAT GGAMDASNLL 

       310        320        330        340        350        360 
KPMLARGELR CIGATTLDEH RQHIEKDPAL ERRFQQVLVD QPTVQDTISI LRGLKERYEV 

       370        380        390        400        410        420 
HHGVRIADNA LVAAAVLSSR YIADRFLPDK AIDLMDESAA RLKMEITSKP EEIDEIDRKI 

       430        440        450        460        470        480 
VQLEMEKLSL GRESDSVSKE RLEKLERELA ELAEQQSALN AQWQQEKGAI DDLSSLKEEI 

       490        500        510        520        530        540 
ERVQLQVEQA KRSYDLNKAA ELEYGTLAGL QKQLSEKETA LAQDGEAGDK SLLREEVTED 

       550        560        570        580        590        600 
DIADVIAKWT GIPVAKLVQS EMEKLLGLEA ELHQRVIGQE QAVQAVADAI QRSRAGLSDP 

       610        620        630        640        650        660 
NRPIASFLFL GPTGVGKTEL SKALASQLFD SEAALVRIDM SEYMEKHSVS RLIGAPPGYV 

       670        680        690        700        710        720 
GYEAGGQLTE AVRRRPYAVI LFDEVEKAHQ DVFNVMLQIL DDGRVTDGQG RTVDFTNTVL 

       730        740        750        760        770        780 
ILTSNIGSQS ILDLGGDDSQ YREMERRVHD ALHAHFRPEF LNRLDETIIF HSLRREELRQ 

       790        800        810        820        830        840 
IVALQVNRLR ERLCDRKLGL EISDTAADWL ANAGYDPVYG ARPLKRAIQR ELETPIAKSI 

       850        860 
LAGLYGDSQI VHVDVDVDQE RLSFR

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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: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX548175 Genomic DNA. Translation: CAE20624.1.
RefSeqNP_894282.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V8B1.
SMRQ7V8B1. Positions 160-343.
ModBaseSearch...

Protein-protein interaction databases

STRING74547.PMT0449.

Proteomic databases

PRIDEQ7V8B1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20624; CAE20624; PMT_0449.
GeneID1729619.
KEGGpmt:PMT0449.
PATRIC23008765. VBIProMar135351_0540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0542.
KOK03695.
OMAIVQLEME.
ProtClustDBCLSK825903.

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.
[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]
TIGRFAMsTIGR03346. chaperone_ClpB. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB_PROMM
AccessionPrimary (citable) accession number: Q7V8B1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 62 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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