ID   CLPB_HAEIN              Reviewed;         856 AA.
AC   P44403;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=HI_0859;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22518.1; -; Genomic_DNA.
DR   PIR; F64098; F64098.
DR   AlphaFoldDB; P44403; -.
DR   SMR; P44403; -.
DR   STRING; 71421.HI_0859; -.
DR   EnsemblBacteria; AAC22518; AAC22518; HI_0859.
DR   KEGG; hin:HI_0859; -.
DR   PATRIC; fig|71421.8.peg.900; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_6; -.
DR   OrthoDB; 9803641at2; -.
DR   PhylomeDB; P44403; -.
DR   BioCyc; HINF71421:G1GJ1-900-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   FunFam; 1.10.1780.10:FF:000003; ATP-dependent chaperone ClpB; 1.
DR   FunFam; 1.10.8.60:FF:000017; ATP-dependent chaperone ClpB; 1.
DR   FunFam; 3.40.50.300:FF:000120; ATP-dependent chaperone ClpB; 1.
DR   FunFam; 3.40.50.300:FF:000025; ATP-dependent Clp protease subunit; 1.
DR   FunFam; 3.40.50.300:FF:000010; Chaperone clpB 1, putative; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_N.
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; IPR050130; ClpA_ClpB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   NCBIfam; NF008118; PRK10865.1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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..856
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191127"
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..545
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          555..764
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          765..856
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          391..523
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         605..612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   856 AA;  95837 MW;  B8958ED9BD03EA3B CRC64;
     MNIEKFTTKF QEALSERQSL AIGKDNQFIE PVHLLTALLN QQGGSIAPIL TASGVNVALL
     RNELKTELNK LPQVIGNGGD VQLSRQLINL LNLCDKFAQQ NQDKFISSEL FLFAALEERG
     TISDILKKCG AKKEQISQAI QHIRGGQNVN DQNAEESRQA LEKYTIDLTA RAESGKLDPV
     IGRDEEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNKRVLSL
     DMGALIAGAK YRGEFEERLK AVLNELSKEE GRVILFIDEI HTMVGAGKTD GAMDAGNLLK
     PSLARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVDE PSVEDTIAIL RGLKERYEIH
     HHVDITDPAI VAAATLSHRY ISDRQLPDKA IDLIDEAASS IRMEIDSKPE PLDRLERRII
     QLKLEQQALQ KEEDEASRKR LEMLEKELAE KEREYAELEE VWKSEKATLS GSQHIKQELD
     TAKTELEQAR RAGDLAKMSE LQYGRIPDLE KQLEQAETSE GKEMTLLRYR VTDEEIAEVL
     SKATGIPVSK MMEGEKEKLL RMEDELHKRV IGQEEAVDAV ANAIRRSRAG LSDPNRPIGS
     FLFLGPTGVG KTELCKTLAK FLFDSEDAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
     YLTEAVRRRP YSVILLDEVE KAHADVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
     GSDLIQGNKD ESYSEMKALV MSVVSQHFRP EFINRIDETV VFHPLGKENI RAIASIQLER
     LAKRMETRGY ELVFTDALLD FIGEVGYDPI YGARPLKRAI QQEIENSLAQ QILSGALLPG
     KVVTIDYANA EVQARQ
//