ID A0A0C1R082_9CYAN Unreviewed; 872 AA.
AC A0A0C1R082;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:KAF3885021.1};
GN ORFNames=DA73_0233145 {ECO:0000313|EMBL:KIE09238.1}, DA73_0400005765
GN {ECO:0000313|EMBL:KAF3885021.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE09238.1};
RN [1] {ECO:0000313|EMBL:KIE09238.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE09238.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3885021.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3885021.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) 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:KIE09238.1}.
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DR EMBL; JHEG04000001; KAF3885021.1; -; Genomic_DNA.
DR EMBL; JHEG02000058; KIE09238.1; -; Genomic_DNA.
DR RefSeq; WP_038088844.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1R082; -.
DR STRING; 1479485.DA73_0233145; -.
DR OrthoDB; 438311at2; -.
DR Proteomes; UP000029738; 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 78, MITOCHONDRIAL; 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:UP000029738};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 6..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..535
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 98737 MW; 21A5614F1C670560 CRC64;
MQPTNPNQFT EKAWEAIAHT PDIAKQYQQQ QIESEHLMKA LLDQEGLANG VFTKAGVNSQ
KLRDRTEQFI QRQPRVSGSS SSVYLGRSLD TLLDRADGYR KEFQDDFISI EHLLLAYAKD
DRFGKGLFQE FGLDEGKVKN IVKQIRGNQK VTDQNPEGKY QSLEKYGRDL TEAARQGKLD
PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIIAGDV PQSLKDRKLI
ALDMGALIAG AKFRGEFEER LKAVLKEVTE SNGNIVLFID EIHTVVGAGA TQGAMDAGNL
LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQQVYV DQPSVEDTIS ILRGLKERYE
VHHGVKISDS SLVAAATLSS RYISDRFLPD KAIDLVDEAA ARLKMEITSK PEELDEIDRK
ILQLEMEKLS LQKESDAASR ERLDRLEKEL ADFKEEQREL KTQWQSEKDV IAKIQSVKEE
IDRVNLEIQQ AERNYDLNRA AELKYGKLTS LHRDLEAAET ELAHAQRSGK SLLREEVTEA
DIAEVISKWT GIPISKLVES EKEKLLHLED ELHNRVVGQE EAVTAVADAI QRSRAGLADP
NRPIASFIFL GPTGVGKTEL AKALAAYLFD TEEALVRIDM SEYMEKHAVS RLIGAPPGYV
GYEEGGQLTE AIRRRPYAVI LFDEIEKAHP DVFNIFLQIL DDGRVTDAQG HTVDFKNSII
IMTSNIGSQY ILDVAGDDSR YDEMRHRVME AMRNSFRPEF LNRLDEIIFF HGLRKEELRR
IVQLQVERLR HRLSDRKMSL RLSEAALDFL ADVGYDPVFG ARPLKRAIQR ELETQIAKAI
LRGEFNDGDT IFVDIENERL AFKRLPTEVF TA
//
