ID A0A0C1N2D0_9CYAN Unreviewed; 873 AA.
AC A0A0C1N2D0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:KAF3890144.1};
GN ORFNames=DA73_0234835 {ECO:0000313|EMBL:KIE06546.1}, DA73_0400035340
GN {ECO:0000313|EMBL:KAF3890144.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE06546.1};
RN [1] {ECO:0000313|EMBL:KIE06546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE06546.1};
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:KAF3890144.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3890144.1};
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:KIE06546.1}.
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DR EMBL; JHEG04000001; KAF3890144.1; -; Genomic_DNA.
DR EMBL; JHEG02000059; KIE06546.1; -; Genomic_DNA.
DR RefSeq; WP_038092426.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1N2D0; -.
DR STRING; 1479485.DA73_0234835; -.
DR OrthoDB; 9803641at2; -.
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 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:UP000029738};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 6..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..536
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 873 AA; 99488 MW; EB4B6479E34C884B CRC64;
MQPTNPEQFT EKAWEALVRT PEIAKQFQHQ QIESEHLMPA LLKQEGLASS IFNKAGVNVQ
KLHERTIDFI NRQPKVSGAS SGSVYIGHSL ETLLDRAEQY RKEFGDEYIS IEHLILAFAK
DDRFGKGLFQ EFGLDEKKLR NIIQQIRGSQ KVTDQNPEVK YEALEKYGRD LTQLAHEGIL
DPVIGRDEEI RRTIQILSRR TKNNPVLIGE PGVGKTAIVE GLAQRIVSGD VPESLRDRKL
IALDMGALIA GAKYRGEFEE RLKAVLKEIQ EAQGQIVLFI DEIHTVVGAG ATQGSMDASN
LLKPMLARGE LRCIGATTLD EYRKYIEKDA ALERRFQQVY VDQPSVEDTI SILRGLKERY
ELHHGVKVSD SALVAAATLS ARYISDRFLP DKAIDLVDEA AAKLKMEITS KPEELDEIDR
KILQLEMERL SLQKETDSAS RERLERLERE LAELKERQDA LNAQWQAEKQ IIDRIRQIRQ
EIERVNVEIQ QAERDYDLNR AAELKYSKLT ELQRQLKEAE ARLAQIQTSG KSLLREEVTE
ADIAEIISKW TGILVSRLVE SEMQKLLHLE EELHKRVIGQ DEAVRAVADA IQRSRAGLAD
PNRPIASFIF LGPTGVGKTE LAKALAEYLF DTEDALVRID MSEYMEKHAV ARLIGAPPGY
VGYEEGGQLT EAIRRRPYSV ILFDEIEKAH PDVFNVLLQI LDDGRLTDSQ GRTVDFKNTI
AIMTSNIGSI YILDVAGDDS KYEQMRDRVM EAVRESFRPE FLNRIDEIII FHSLRKDELR
EIVKLQVQHL EERLRERKLL LKISDEALDW IVQVGYDPVY GARPLKRAIQ RELETPIAKA
ILRGEFHEGD TIYVHVEHER LVLKCLSPEL VNA
//