ID B5IL34_9CYAN Unreviewed; 883 AA.
AC B5IL34;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EDY38597.1};
GN ORFNames=CPCC7001_1476 {ECO:0000313|EMBL:EDY38597.1};
OS Cyanobium sp. PCC 7001.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=180281 {ECO:0000313|EMBL:EDY38597.1, ECO:0000313|Proteomes:UP000003950};
RN [1] {ECO:0000313|EMBL:EDY38597.1, ECO:0000313|Proteomes:UP000003950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7001 {ECO:0000313|EMBL:EDY38597.1,
RC ECO:0000313|Proteomes:UP000003950};
RA Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; DS990556; EDY38597.1; -; Genomic_DNA.
DR RefSeq; WP_006910499.1; NZ_DS990556.1.
DR AlphaFoldDB; B5IL34; -.
DR STRING; 180281.CPCC7001_1476; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000003950; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 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_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 NCBIfam; TIGR03346; chaperone_ClpB; 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; 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; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000003950};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 5..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..500
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 883 AA; 97380 MW; 6A43B7B43DCC6704 CRC64;
MHPTAELFTE KAWGAVVAAQ QLAVQKRQQQ MESEHLFAAL LAQQGLAGRI LEKAGVDVGG
LSQKVDAFMA GQPSLSAPPD NVYLGKGLNS VLDQADQLKQ SYGDSYIAVE HLLLALAIDD
RCGKQLLSQA GTNADKLKEA VQAVRGSQTV TDQNPEGTYE SLEKYGRDLT AAARDGKLDP
VIGRDEEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP QALQNRQLIA
LDMGALIAGA KYRGEFEERL KAVLKEVTSS EGQIVLFIDE IHTVVGAGAT GGAMDASNLL
KPMLARGELR CIGATTLDEH RQHIEKDPAL ERRFQQVFVD QPTVEDTISI LRGLKERYEV
HHGVRIADNA LVAAAVLSSR YIADRFLPDK AIDLVDESAA RLKMEITSKP EEIDELDRRI
LQLEMEKLSL GRESDSASKD RLERLERELA ELREQQSTLN AQWQAEKGSI DALSALKEEI
EQVQLQVEQA KRQYDLNKAA ELEYGTLAEL HKRLAAKEAE LSEGNGSGEK SLLREEVTED
DIAEVIAKWT GIPVSRLVQS EMEKLLHLEE ELHTRVIGQE QAVTAVADAI QRSRAGLSDP
NRPIASFLFL GPTGVGKTEL SKALAAQLFD SDEAMVRIDM SEYMEKHAVS RLIGAPPGYV
GYEEGGQLTE AVRRRPYAVI LFDEVEKAHP DVFNVMLQIL DDGRVTDGQG RTVDFTNTVL
ILTSNIGSSS ILDLAGDPAR HGEMEKRVND ALRAHFRPEF LNRLDETIIF HSLKQEELRE
IVELQVKRLE RRLDDRKLGL ALNADALDWL AGVGYDPVYG ARPLKRAIQR ELETPIAKAI
LAGEFTPGHT ITVDVVEASN GSEGPQRRLR FQQSDPAQLP VLV
//