CLPB_STAES
ID CLPB_STAES Reviewed; 869 AA.
AC Q8CPT5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=SE_0674;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(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; AE015929; AAO04271.1; -; Genomic_DNA.
DR RefSeq; NP_764229.1; NC_004461.1.
DR RefSeq; WP_001829334.1; NZ_WBME01000074.1.
DR AlphaFoldDB; Q8CPT5; -.
DR SMR; Q8CPT5; -.
DR STRING; 176280.SE_0674; -.
DR EnsemblBacteria; AAO04271; AAO04271; SE_0674.
DR KEGG; sep:SE_0674; -.
DR PATRIC; fig|176280.10.peg.648; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; GPEHILM; -.
DR Proteomes; UP000001411; 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; Repeat;
KW Stress response.
FT CHAIN 1..869
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191181"
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 85..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..549
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 442..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..771
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 772..869
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 390..524
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 609..616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 869 AA; 98187 MW; 53EDE4130AD420E3 CRC64;
MDINQMTYAV QGALQKAVAY SKEYELQNIE VEALLKAAMN ENDSLFKSIL ERANIDVDQL
IKAYDNQLSH YPTVQGDNVQ YGQYISAKTN ELLDKAEKYM KSYEDEFISM EHILRAAIDT
DETTQKWVGN KVEVIKEIIT KVRGGNHVTS QNPEVNYEAL EKYGRDLVEE VRQGKMDPVI
GRDEEIRNTI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVRKDVPES LLDKTIFELD
LSALVAGAKY RGEFEERLKA VLKEVKESEG RIILFIDEIH MLVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLNEYRE YIEKDSALER RFQKVGVSEP DVEDTISILR GLKERYEVYH
GVRIQDRALV AAAELSDRYI TDRFLPDKAI DLVDQACATI RTEMGSNPTE LDQVNRRVMQ
LEIEESALKN ESDNASKHRL EELQEELSNE KEKQSSLKSR VEQEKEKIAK VQEKRAELDS
SRQALEDAQT EGNLEKAAEL QYGTIPQLEK ELQEFEEAFQ DETGEDSERM IREVVSDEEI
GDIVSQWTGI PVSKLVETER EKLLSLSDIL HKRVVGQDKA VDLVSDAVVR ARAGIKDPNR
PIGSFLFLGP TGVGKTELAK SLASSLFDSE KHMIRIDMSE YMEKHAVSRL IGAPPGYVGH
DEGGQLTEAV RRNPYSVILL DEVEKAHSDV FNVLLQILDE GRLTDSKGRS VDFKNTIIIM
TSNIGSQVLL ENVKDAGEIS DDTEKAVMDS LHAYFKPEIL NRMDDIVLFK PLSVNDMSMI
VDKILTQLNM RLLDQHISIE VTEEAKKWLG EEAYEPQFGA RPLKRFVQRQ IETPIARMMI
KESLPEGTII KVDLNDNKEL DFKVVKPTS
