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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Vibrio vulnificus (strain CMCP6)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Nucleotide bindingi206 – 213ATP 1By similarity8
Nucleotide bindingi605 – 612ATP 2By similarity8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciVVUL216895:G1GJ4-472-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein ClpB
Gene namesi
Name:clpB
Ordered Locus Names:VV1_0482
OrganismiVibrio vulnificus (strain CMCP6)
Taxonomic identifieri216895 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001912021 – 857Chaperone protein ClpBAdd BLAST857

Proteomic databases

PRIDEiQ8DEV2

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ8DEV2
SMRiQ8DEV2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 143N-terminalBy similarityAdd BLAST143
Regioni159 – 340NBD1By similarityAdd BLAST182
Regioni341 – 545LinkerBy similarityAdd BLAST205
Regioni555 – 765NBD2By similarityAdd BLAST211
Regioni766 – 857C-terminalBy similarityAdd BLAST92

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili391 – 525By similarityAdd BLAST135

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
OMAiHHKVRIK
OrthoDBiPOG091H019M

Family and domain databases

Gene3Di1.10.1780.10, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR017730 Chaperonin_ClpB
IPR019489 Clp_ATPase_C
IPR004176 Clp_N
IPR036628 Clp_N_dom_sf
IPR001270 ClpA/B
IPR018368 ClpA/B_CS1
IPR028299 ClpA/B_CS2
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF07724 AAA_2, 1 hit
PF02861 Clp_N, 2 hits
PF10431 ClpB_D2-small, 1 hit
PRINTSiPR00300 CLPPROTEASEA
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SM01086 ClpB_D2-small, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF81923 SSF81923, 1 hit
TIGRFAMsiTIGR03346 chaperone_ClpB, 1 hit
PROSITEiView protein in PROSITE
PS00870 CLPAB_1, 1 hit
PS00871 CLPAB_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q8DEV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLDRFTSKF QIAISDAQSL ALGRDHQYIE PVHLMVALLD QNGSPIRPLL
60 70 80 90 100
TILNVDVTHL RSKLSEMLDR LPKVSGIGGD VQLSSAMGAM FNLCDKIAQK
110 120 130 140 150
RQDAYISSEI FLLAAIEDRG PLGQLFKELG LTEQKVSQAI EQIRGGQKVN
160 170 180 190 200
DQNAEELRQA LEKFTIDLTE RAEQGKLDPV IGRDDEIRRT IQVLQRRTKN
210 220 230 240 250
NPVIIGEPGV GKTAIVEGLA QRIINNEVPE GLRGRRVLSL DMGALVAGAK
260 270 280 290 300
YRGEFEERLK SVLNELSKEE GNIILFIDEL HTMVGAGKGE GSMDAGNMLK
310 320 330 340 350
PALARGELHC VGATTLDEYR QYIEKDPALE RRFQKVLVDE PTVEDTIAIL
360 370 380 390 400
RGLKERYELH HHVEITDPAI VAAASLSHRY VSDRQLPDKA IDLIDEAASS
410 420 430 440 450
IRMQIDSKPE ALDKLERKII QLKIEQQALS NEHDEASEKR LRSLNEELNE
460 470 480 490 500
KEREFAELEE IWNAEKAALS GTQHIKAALE QARMDMEFAR RAGDLSRMSE
510 520 530 540 550
LQYGRIPELE KQLDLATQAE MQEMTLLKNK VTDNEIAEVL SKQTGIPVSK
560 570 580 590 600
MLEAEKEKLL RMEEVLHKRV IGQKEAVEVV ANAIRRSRAG LSDPNKPIGS
610 620 630 640 650
FLFLGPTGVG KTELCKTLAN FMFDSEDAMV RIDMSEFMEK HSVARLVGAP
660 670 680 690 700
PGYVGYEEGG YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT
710 720 730 740 750
DGQGRTVDFR NTVVIMTSNL GSSRIQENFA MLDYQGIKEQ VMEVVTKHFR
760 770 780 790 800
PEFLNRVDET VVFHPLGQDH IKSIAAIQLN RLANRMEEHG YPLEVSDKAL
810 820 830 840 850
ELIAQVGFDP VYGARPLKRA IQQSIENPLA KSILAGSVLP DKKIQLIVNN

DQIVAHQ
Length:857
Mass (Da):96,036
Last modified:March 1, 2003 - v1
Checksum:i813C329C777F68E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016795 Genomic DNA Translation: AAO09001.1
RefSeqiWP_011078571.1, NC_004459.3

Genome annotation databases

EnsemblBacteriaiAAO09001; AAO09001; VV1_0482
KEGGivvu:VV1_0482

Similar proteinsi

Entry informationi

Entry nameiCLPB_VIBVU
AccessioniPrimary (citable) accession number: Q8DEV2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: March 1, 2003
Last modified: March 28, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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