CLPB_NITEU
ID CLPB_NITEU Reviewed; 863 AA.
AC Q82SD8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=NE2402;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD86314.1; -; Genomic_DNA.
DR RefSeq; WP_011112875.1; NC_004757.1.
DR AlphaFoldDB; Q82SD8; -.
DR SMR; Q82SD8; -.
DR STRING; 228410.NE2402; -.
DR PRIDE; Q82SD8; -.
DR EnsemblBacteria; CAD86314; CAD86314; NE2402.
DR KEGG; neu:NE2402; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_4; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR PhylomeDB; Q82SD8; -.
DR Proteomes; UP000001416; 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..863
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191149"
FT DOMAIN 3..146
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 83..146
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..340
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 341..550
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..769
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 770..863
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 391..525
FT /evidence="ECO:0000250"
FT BINDING 206..213
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 863 AA; 96346 MW; 6733DEC24C42AC01 CRC64;
MRFDKFTTKF QQALADAQSM ALGQDHPYIE PQHLLLALMQ QDDGSITSLL QRAGVNAQPL
RQALTQSLKL LPKVEGTGGE INVSRDLANL LNLTDKEAQK RGDQYIASEM FLLAALEDKG
ETGRLLKQYG ATRAALEQAV DSVRGGEKVT DAEAEGSREA LKKYTLDLTE RARSGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE TLKNKRVLSL
DMAALLAGAK YRGEFEERLK AVLKELAQDE GRTIVFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR KYVEKDAALE RRFQKVLVDE PGVEATIAIL RGLQEKYELH
HGVEITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IRMEQDSKPE VMDKLDRRLI
QLKIEREAVR KEKDDASKKR LALLEEEISK LEREYADLDE ILKAEKSRAK GSQEIKEELD
KLRREEEAAR RKGDLQRASE LLYGRIPQLE AQLAEQLHHA ESAEEAVQPK LFRTQVGAEE
IAEVVSRATG IPVSKMMQGE REKLLFMEDK LHERVIGQDE AVRLVSDAIR RSRSGLADPN
RPYGSFLFLG PTGVGKTELC KALAGFLFDS EEHLIRVDMS EFMEKHSVAR LIGAPPGYVG
YEEGGYLTEQ VRRKPYSVIL LDEVEKAHPD VFNVLLQVLD DGRMTDGQGR TVDFKNTVIV
MTSNLGSQMI QQMSGDDYQV IKLAVMGEVK TYFRPEFINR IDEVVVFHAL GEAHIKSIAR
IQLSNLGKRL AQMEMKLVVS EPALTKLAEV GFDPVFGARP LKRAIQAQIE NPLAKELLEG
HFSAGDTILV EYSNGHMQFT AQR
