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Database: UniProt
Entry: Q05RB2_9SYNE
LinkDB: Q05RB2_9SYNE
Original site: Q05RB2_9SYNE 
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
//
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