CLPB_PASMU
ID CLPB_PASMU Reviewed; 855 AA.
AC Q9CKC0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=PM1704;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004439; AAK03788.1; -; Genomic_DNA.
DR RefSeq; WP_005755290.1; NC_002663.1.
DR AlphaFoldDB; Q9CKC0; -.
DR SMR; Q9CKC0; -.
DR STRING; 747.DR93_657; -.
DR PRIDE; Q9CKC0; -.
DR EnsemblBacteria; AAK03788; AAK03788; PM1704.
DR KEGG; pmu:PM1704; -.
DR PATRIC; fig|272843.6.peg.1725; -.
DR HOGENOM; CLU_005070_1_0_6; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000000809; 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..855
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191152"
FT DOMAIN 3..145
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..145
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 158..339
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 340..544
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 554..763
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 764..855
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 390..522
FT /evidence="ECO:0000250"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 855 AA; 95396 MW; 6ABB2DBBB23E498B CRC64;
MNIEKFTTKF QQALQEAQSL AIGKDNQFIE PVHLLTALLN QQGGSTAPIL TASGANLPLL
RNELNAELSK LPQVSGSGGD VQVSRSLVNL LNLCDKLAQQ RQDKFISSEL FLLAALEDKT
LGDVLKKCGV KKENLQQAIE KVRGGQNVND PNAEESRQAL EKYTIDLTAR AESGKLDPVI
GRDEEIRRAI QVLQRRTKNN PVLIGEPGVG KTAIVEGLAQ RIVNGEVPEG LKNKRVLSLD
MGALIAGAKY RGEFEERLKA VLNELSKEEG RVILFIDEIH TMVGAGKTDG AMDAGNLLKP
SLARGELHCV GATTLDEYRQ YIEKDAALER RFQKVFVGEP TVEDTIAILR GLKERYEIHH
HVQITDPAIV AAATLSHRYV SDRQLPDKAI DLIDEAASSI RMEIDSKPQP LDRLERRIIQ
LKLEQQALQK EDDDASRKRL AMLEKELGEK EREYAELEDV WKAEKAALSG TQHIKAELDS
AKTQMEQARR ASDFAKMSEL QYGVIPALEK QLAQAESAEG KEMTLLRYRV TDEEIAEVLS
RATGIPVAKM MEGEKEKLLR MEEELHKRVI GQHEAIEAVS NAIRRSRAGL SDPNRPIGSF
LFLGPTGVGK TELCKTLANF LFDDENAMVR IDMSEFMEKH SVSRLVGAPP GYVGYEEGGY
LTEAVRRRPY SVILLDEVEK AHHDVFNILL QVLDDGRLTD GQGRTVDFRN TVVIMTSNLG
SHLIQENSTL DYPSMKELVM SVVGQHFRPE FINRIDETVV FHPLGKENIR EIATIQLARL
IKRMESHGYQ LHFTDACLDF IGEVGYDPVY GARPLKRAIQ QEIENPLAQQ ILSGKLLPNQ
LVTIDYVDGK VIANQ
