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P44403 (CLPB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. 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
Gene names
Name:clpB
Ordered Locus Names:HI_0859
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length856 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 – 856856Chaperone protein ClpB
PRO_0000191127

Regions

Nucleotide binding206 – 2138ATP 1 By similarity
Nucleotide binding605 – 6128ATP 2 By similarity
Region1 – 143143N-terminal By similarity
Region159 – 340182NBD1 By similarity
Region341 – 545205Linker By similarity
Region555 – 764210NBD2 By similarity
Region765 – 85692C-terminal By similarity
Coiled coil391 – 523133 By similarity

Sequences

Sequence LengthMass (Da)Tools
P44403 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B8958ED9BD03EA3B

FASTA85695,837
        10         20         30         40         50         60 
MNIEKFTTKF QEALSERQSL AIGKDNQFIE PVHLLTALLN QQGGSIAPIL TASGVNVALL 

        70         80         90        100        110        120 
RNELKTELNK LPQVIGNGGD VQLSRQLINL LNLCDKFAQQ NQDKFISSEL FLFAALEERG 

       130        140        150        160        170        180 
TISDILKKCG AKKEQISQAI QHIRGGQNVN DQNAEESRQA LEKYTIDLTA RAESGKLDPV 

       190        200        210        220        230        240 
IGRDEEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNKRVLSL 

       250        260        270        280        290        300 
DMGALIAGAK YRGEFEERLK AVLNELSKEE GRVILFIDEI HTMVGAGKTD GAMDAGNLLK 

       310        320        330        340        350        360 
PSLARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVDE PSVEDTIAIL RGLKERYEIH 

       370        380        390        400        410        420 
HHVDITDPAI VAAATLSHRY ISDRQLPDKA IDLIDEAASS IRMEIDSKPE PLDRLERRII 

       430        440        450        460        470        480 
QLKLEQQALQ KEEDEASRKR LEMLEKELAE KEREYAELEE VWKSEKATLS GSQHIKQELD 

       490        500        510        520        530        540 
TAKTELEQAR RAGDLAKMSE LQYGRIPDLE KQLEQAETSE GKEMTLLRYR VTDEEIAEVL 

       550        560        570        580        590        600 
SKATGIPVSK MMEGEKEKLL RMEDELHKRV IGQEEAVDAV ANAIRRSRAG LSDPNRPIGS 

       610        620        630        640        650        660 
FLFLGPTGVG KTELCKTLAK FLFDSEDAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG 

       670        680        690        700        710        720 
YLTEAVRRRP YSVILLDEVE KAHADVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL 

       730        740        750        760        770        780 
GSDLIQGNKD ESYSEMKALV MSVVSQHFRP EFINRIDETV VFHPLGKENI RAIASIQLER 

       790        800        810        820        830        840 
LAKRMETRGY ELVFTDALLD FIGEVGYDPI YGARPLKRAI QQEIENSLAQ QILSGALLPG 

       850 
KVVTIDYANA EVQARQ

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22518.1.
PIRF64098.
RefSeqNP_439019.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44403.
SMRP44403. Positions 4-141, 159-351.
ModBaseSearch...

Protein-protein interaction databases

STRING71421.HI0859.

Proteomic databases

PRIDEP44403.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22518; AAC22518; HI_0859.
GeneID949871.
KEGGhin:HI0859.
PATRIC20190373. VBIHaeInf48452_0900.

Phylogenomic databases

eggNOGCOG0542.
KOK03695.
OMALIQDRFG.
ProtClustDBCLSK870580.

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_HAEIN
AccessionPrimary (citable) accession number: P44403
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

SIMILARITY comments

Index of protein domains and families

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