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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed-Annotation score: 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 bindingi207 – 2148ATP 1By similarity
Nucleotide bindingi608 – 6158ATP 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciCEFF196164:GJW8-2668-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein ClpB
Gene namesi
Name:clpB
Ordered Locus Names:CE2613
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000001409 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 852852Chaperone protein ClpBPRO_0000191115Add
BLAST

Proteomic databases

PRIDEiQ8FM94.

Interactioni

Subunit structurei

Homohexamer. The oligomerization is ATP-dependent (By similarity).By similarity

Protein-protein interaction databases

STRINGi196164.HMPREF0290_0256.

Structurei

3D structure databases

ProteinModelPortaliQ8FM94.
SMRiQ8FM94. Positions 160-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 144144N-terminalBy similarityAdd
BLAST
Regioni160 – 342183NBD1By similarityAdd
BLAST
Regioni343 – 548206LinkerBy similarityAdd
BLAST
Regioni558 – 756199NBD2By similarityAdd
BLAST
Regioni757 – 85296C-terminalBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili393 – 527135By 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

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
KOiK03695.
OMAiGDEYTST.
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.
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.
SSF81923. SSF81923. 1 hit.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8FM94-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFNPTTKT SEAMQAALQQ ASANGNPDIR PAHLLVAILD QADGVAAPVL
60 70 80 90 100
TAAGVDPKTI LAEAQKLVDG YPKASGSNLA NPNFNRDALN ALTASQELAG
110 120 130 140 150
ELGDEYVSTE VLLAGIARGK SDAADLLKGK GATYDAIKAA FQSVRGSQKV
160 170 180 190 200
TSQDPEGQFQ ALEKYSTDLT KLAREGKIDP VIGRDQEIRR VVQVLSRRTK
210 220 230 240 250
NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP ESLKGKTLIS LDLGSMVAGA
260 270 280 290 300
KYRGEFEERL KAVLDEIKGA NGEIVTFIDE LHTIVGAGAS GESAMDAGNM
310 320 330 340 350
IKPLLARGEL RLVGATTLNE YRKYIEKDTA LERRFQQVYV GEPSVEDTVG
360 370 380 390 400
ILRGLKERYE VHHGVRIQDS ALVAAAELSH RYITSRFLPD KAIDLVDEAA
410 420 430 440 450
SRLRMEIDSS PQEIDELERI VRRLEIEEVA LTKETDVASR ERLERLRSEL
460 470 480 490 500
ADEREKLSEL KARWQNEKAV IDDVRKFKEE LEALRSESDI AEREGDYGRV
510 520 530 540 550
AELRYGRIPE LEKKIAEAEE KIGGADNSML TEEVTPEVIA EVVSAWTGIP
560 570 580 590 600
AGKMMQGETE KLLNMERFLG KRVVGQHEAV TAVSDAVRRS RAGVADPNRP
610 620 630 640 650
TGSFLFLGPT GVGKTELAKA VSEFLFDDER AMVRIDMSEY SEKHSVARLV
660 670 680 690 700
GAPPGYVGYD QGGQLTEAVR RRPYTTVLFD EVEKAHPDVF DILLQVLDDG
710 720 730 740 750
RLTDGQGRTV DFRNTILILT SNLGAGGTRE QMMDAVKMAF KPEFINRLDD
760 770 780 790 800
IVVFDPLSQE QLASIVEIQI SQLAERLSDR RLTLRVSDAA KLWLAERGYD
810 820 830 840 850
PAYGARPLRR LIQQAIGDQL AKELLAGEIR DGDRVLVDVA DGGQYLAVSR

EH
Length:852
Mass (Da):93,445
Last modified:March 1, 2003 - v1
Checksum:i426359F92D8BAB0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC19423.1.
RefSeqiWP_011076009.1. NZ_GG700685.1.

Genome annotation databases

EnsemblBacteriaiBAC19423; BAC19423; BAC19423.
KEGGicef:CE2613.
PATRICi21491373. VBICorEff9312_2580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC19423.1.
RefSeqiWP_011076009.1. NZ_GG700685.1.

3D structure databases

ProteinModelPortaliQ8FM94.
SMRiQ8FM94. Positions 160-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_0256.

Proteomic databases

PRIDEiQ8FM94.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC19423; BAC19423; BAC19423.
KEGGicef:CE2613.
PATRICi21491373. VBICorEff9312_2580.

Phylogenomic databases

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
KOiK03695.
OMAiGDEYTST.
OrthoDBiEOG65F8SM.

Enzyme and pathway databases

BioCyciCEFF196164:GJW8-2668-MONOMER.

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.
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.
SSF81923. SSF81923. 1 hit.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiCLPB_COREF
AccessioniPrimary (citable) accession number: Q8FM94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: March 1, 2003
Last modified: January 20, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.