CLPB1_THEVB
ID CLPB1_THEVB Reviewed; 871 AA.
AC Q8DJ40;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Chaperone protein ClpB 1;
GN Name=clpB1; OrderedLocusNames=tlr1389;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08941.1; -; Genomic_DNA.
DR RefSeq; NP_682179.1; NC_004113.1.
DR RefSeq; WP_011057229.1; NC_004113.1.
DR AlphaFoldDB; Q8DJ40; -.
DR SMR; Q8DJ40; -.
DR STRING; 197221.22295113; -.
DR PRIDE; Q8DJ40; -.
DR EnsemblBacteria; BAC08941; BAC08941; BAC08941.
DR KEGG; tel:tlr1389; -.
DR PATRIC; fig|197221.4.peg.1461; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000440; 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..871
FT /note="Chaperone protein ClpB 1"
FT /id="PRO_0000191187"
FT DOMAIN 6..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 9..73
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 84..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..550
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 560..771
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 772..871
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..526
FT /evidence="ECO:0000250"
FT BINDING 207..214
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 871 AA; 98389 MW; D19D08E1A680F5FB CRC64;
MQPSNPNQFT EKAWAAIART PDLAKQAQHQ NLESEHLMKS LLEQEGLATQ IFQKAGCSVQ
RIRDLTDEFI SRQPKISHPS GVYLGQSLDK LLDRAEEARK QFGDEFISIE HLVLAFAQDD
RFGKKLFQDI GLSEKVLREA IQQIRGSQKV TDQNPEGKYA ALEKYGRDLT LLARQGKLDP
VIGRDDEIRR VIQILSRRTK NNPVLIGEPG VGKTAIAEGL AQRIVARDVP DSLRDRQLIA
LDMGALIAGA KYRGEFEERL KAVLKEVTDS NGQIILFIDE IHTVVGAGAT QGAMDAGNLL
KPMLARGELR CIGATTLDEY RKYIEKDAAL ERRFQQVYVD QPSVEDTISI LRGLKERYEI
HHGVKISDTA LVAAATLSAR YISDRFLPDK AIDLVDEAAA KLKMEITSKP EELDEIDRKI
LQLEMERLSL QKETSAASRD RLEKLERELA DLKEEQSRLN AQWQAEKEVI DRLQSIKEEI
EKVNIEIQQA ERNYDLNRAA ELKYGKLTEL HKKLAEAEAK LREIQVGGRS LLRDEVTEAD
IAEIISKWTG IPVSKLVESE AQKLLHLEEE LHKRVVGQDE AVSAVAEAIQ RSRAGLADPN
RPIASFIFLG PTGVGKTELA KALAAFMFDT EEALVRIDMS EYMEKHAVSR LIGAPPGYVG
YDEGGQLTEA IRRRPYAVVL FDEIEKAHPD VFNVFLQILD DGRVTDSQGR TVDFKNTIII
MTSNIGSQYI LDVAGDDSRY SEMYNRVMEA MRAHFRPEFL NRVDEFIIFH SLRKDQLRQI
VQLQVQRLQQ RLSDRHITLS LTEKAIDFLA EVGYDPVYGA RPLKRAIQKQ LETPIAKAIL
RGDFFDGDTI LVDVGEDERL SFRRQVELAT V