ID A0A161KJU2_9SYNE Unreviewed; 874 AA.
AC A0A161KJU2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=FLM9_1005 {ECO:0000313|EMBL:CZB19333.1};
OS Candidatus Synechococcus spongiarum.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=431041 {ECO:0000313|EMBL:CZB19333.1, ECO:0000313|Proteomes:UP000182631};
RN [1] {ECO:0000313|Proteomes:UP000182631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA liu f.;
RL Submitted (FEB-2016) 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. {ECO:0000256|RuleBase:RU362034}.
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; FITM01000107; CZB19333.1; -; Genomic_DNA.
DR RefSeq; WP_074457483.1; NZ_FITM01000107.1.
DR AlphaFoldDB; A0A161KJU2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000182631; 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:UP000182631};
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 REGION 853..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..527
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 97113 MW; A02983DAE1CAD84C CRC64;
MQPTPETFTL KAWEAVSSAH TLAKARKSQT LESEHLLKAL LEQKDLAVRI LEAAAVDVAA
LDSNLEQFLA RQPKLGAPPD TVSLGSSLDQ LLDRAEKEQQ AWKDQFIATE HLVLALCEDS
RCGKTLLQAL GGRRQAIKDA VQSIRGNQRV TSQSPEATYE ALQNYGCDLT EAARQGKLDP
VIGRDEEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEAL AQRIVNGDVP TALQNRRLVS
LDMGALIAGA KYRGEFEERL KAVLKEVTSG KDQIVLFIDE VHTVVGAGAA GGSMDASNLL
KPMLARGELR CIGATTLDEH RRYIEKDAAL ERRFQQVVVP QPTVEDTISI LRGLKERYEV
HHGVRIADNA LVAAAVLSSR YINDRFLPDK AIDLVDEAAA HLKTEITSKP EEIDEIDRKI
LQLEMEKLSL AKESDAASRE RLTRINQDLA NLTEQQRALM AQWTQEKGAL DDLQGLKEQI
EQVQVKLEQA KRNYDLNKAA ELEYGTLAEL QQRLQKGEQQ LQDNEKRLLR QTISEEDVAE
VVSKWTGIPV QRLAQSELQK LLDLEQRLQA RVVGQQEAVG SVADAIQRSR AGLADPRRPI
ASFLFLGPTG VGKTELCKAL AEQLFDDEAA IVRLDMSEYM ERHAVSRLIG APPGYVGHEE
GGQLTEAVRR KPYAVILLDE VEKAHPEVFN VLLQVLDDGR ITDSQGRTVN FTNSIVILTS
NIASQAILDL AGDDSRHGEM EARVKQALGT HFRPEFLNRI DEIIIFHALR KQELRRIVEL
QVTQLQQRLQ EKGLSLVLIP EACDWLAAVG YDPVYGARPL RRAIQKHLET PMAKAILRGD
FRKGDTIVVE PEEGRGSQLR MGKGAHPEMV TAAR
//