CLPB_DESVH
ID CLPB_DESVH Reviewed; 865 AA.
AC Q72AW6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=DVU_1874;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AE017285; AAS96350.1; -; Genomic_DNA.
DR RefSeq; WP_010939160.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_011091.1; NC_002937.3.
DR AlphaFoldDB; Q72AW6; -.
DR SMR; Q72AW6; -.
DR STRING; 882.DVU_1874; -.
DR PaxDb; Q72AW6; -.
DR PRIDE; Q72AW6; -.
DR EnsemblBacteria; AAS96350; AAS96350; DVU_1874.
DR KEGG; dvu:DVU_1874; -.
DR PATRIC; fig|882.5.peg.1716; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_7; -.
DR OMA; ERMKAVM; -.
DR PhylomeDB; Q72AW6; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..865
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191119"
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 86..151
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 164..345
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 346..550
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 560..772
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 773..865
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 396..530
FT /evidence="ECO:0000250"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 610..617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 865 AA; 97211 MW; 53750EFBAD4AF619 CRC64;
MDIGKFTEKS QQALAEAQNI AVRFGHQEVD AEHLADALVR QEQGLVPRLL DRMGQKPEAF
AEALERELGK RPAVSGPGAA PGQIFVSKRL NAVLVKAQDF ARQLKDEYVS VEHIFCVLLE
EPASTIMGRI AREFSLSREK VLGVLEDVRG SQRVTSANPE DTYEALQKYG RDLVEEARKG
KLDPVIGRDA EIRRVIRILS RRTKNNPVLI GEAGVGKTAI VEGLAHRILK GDVPEGLKER
GLFALDMGAL IAGAKYRGEF EERLKAVLKE VEKSEGRIIM FIDELHTIVG AGKTDGAMDA
SNLLKPMLAR GELHCIGATT LDEYRKYIEK DPALERRFQP VLVDEPTIED AISILRGLKE
RFEVHHGVRI SDSAIVEAVT LSHRYITDRQ LPDKAIDLID EAAALIRTEI DSLPADLDEA
NRKIMQLEIE REALRRETDV ASRERLERLE NELADLRAEQ TALLSQWERE KGSIDHVRSI
KEDIERTRHA IEEAERAYDL NRAAELKYSR LLELERQLES AEKGGHDETR LLKEEVRPDD
IAEIVARWTG IPVTRLLESE REKLLRLADV LHERVVGQEE AVDAVSEAVL RARAGLSDPS
RPIGSFIFLG PTGVGKTELC KTLAEALFDT EENIVRLDMS EYMEKHAVAR LIGAPPGYVG
YDEGGQLTEA VRRKPYSVVL FDEVEKAHPD VFNTLLQILD DGRLTDSHGR TVDFRNTIII
MTSNIGSPYM LDGISEGGEF LSGVREKVME ELRRHFRPEF LNRVDETVLF KPLLPAQIAR
IVELLLGRLR GRLAERKIDI RLGDVARDFI AKAAYDPVYG ARPLRRYLQH NIETPLARKL
IAGELRDGTT VEVDVVDDAL SFRIE
