CLPB_HAEIN
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 03-AUG-2022, entry version 131.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=HI_0859;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC 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 RefSeq; NP_439019.1; NC_000907.1.
DR RefSeq; WP_010869072.1; NC_000907.1.
DR AlphaFoldDB; P44403; -.
DR SMR; P44403; -.
DR STRING; 71421.HI_0859; -.
DR PRIDE; P44403; -.
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 OMA; SKMMQGE; -.
DR PhylomeDB; P44403; -.
DR BioCyc; HINF71421:G1GJ1-900-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; 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..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
