ID Q05RB2_9SYNE Unreviewed; 877 AA.
AC Q05RB2;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=RS9916_27694 {ECO:0000313|EMBL:EAU73368.1};
OS Synechococcus sp. RS9916.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=221359 {ECO:0000313|EMBL:EAU73368.1, ECO:0000313|Proteomes:UP000004972};
RN [1] {ECO:0000313|EMBL:EAU73368.1, ECO:0000313|Proteomes:UP000004972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS9916 {ECO:0000313|EMBL:EAU73368.1,
RC ECO:0000313|Proteomes:UP000004972};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2006) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU73368.1}.
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DR EMBL; AAUA01000003; EAU73368.1; -; Genomic_DNA.
DR RefSeq; WP_007097476.1; NZ_DS022299.1.
DR AlphaFoldDB; Q05RB2; -.
DR STRING; 221359.RS9916_27694; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_3; -.
DR Proteomes; UP000004972; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:EAU73368.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EAU73368.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004972};
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 435..500
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 877 AA; 96623 MW; F76D5D2FD2C36967 CRC64;
MQPTAELFTE KAWGAIVAAQ QLAQSHRHQQ LESEHLFLAL LEQNGLAGRI LEKAGVSPPE
LQSVVEQHLH QQPALQNRPE SVYLGKGLSD LLDRADALKQ GYGDSFIAIE HLVLALADDS
RCGKRLLNQV GADATSLKTA IDAVRGSQTV TDQNPEGTYE SLEKYGRDLT AAARDGKLDP
VIGRDEEIRR TIQILSRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNGDVP QALQNRQLIA
LDMGALIAGA KYRGEFEERL KAVLKEVTSS EGRIVLFIDE IHTVVGAGAT GGAMDASNLL
KPMLARGELR CIGATTLDEH RQHIEKDPAL ERRFQQVLVD QPTVEDTISI LRGLKERYEV
HHGVRIADSA LVAAAVLSTR YIADRFLPDK AIDLVDESAA RLKMEITSKP EEIDEIDRKI
LQLEMEKLSL GRESDAASQE RLERLEREVA ELSEQQSTLN AQWQQEKGAI DDLSNLKEEI
ERVQLQVEQA KRNYDLNKAA ELEYGTLAGL QKQLSDQEAA LAAADDGGQD KSLLREEVTE
DDIAEVIAKW TGIPVAKLVQ SEMEKLLSLE SQLHERVVGQ QQAVTAVADA IQRSRAGLSD
PNRPIASFLF LGPTGVGKTE LSKALAAQLF DSDDAMVRID MSEYMEKHSV SRLIGAPPGY
VGYEAGGQLT EAIRRRPYSV VLFDEVEKAH PDVFNVMLQI LDDGRVTDGQ GRTVDFTNAV
LILTSNIGSQ SILDLGGDDS QHSEMERRVN EALRAHFRPE FLNRLDDQII FHSLRREELR
QIVSLQVERL RHRLSDRKLS LTISEGATDW LANAGYDPVY GARPLKRAIQ RELETPIAKA
ILGGHYGEGA TVEVDAIAIA GDTGSTDGDA HKQLVLR
//