ID A0A1Z4V8E1_9CYAN Unreviewed; 872 AA.
AC A0A1Z4V8E1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=NIES806_37990 {ECO:0000313|EMBL:BAZ87569.1};
OS Dolichospermum compactum NIES-806.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Dolichospermum; Dolichospermum compactum.
OX NCBI_TaxID=1973481 {ECO:0000313|EMBL:BAZ87569.1, ECO:0000313|Proteomes:UP000218702};
RN [1] {ECO:0000313|EMBL:BAZ87569.1, ECO:0000313|Proteomes:UP000218702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-806 {ECO:0000313|EMBL:BAZ87569.1,
RC ECO:0000313|Proteomes:UP000218702};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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:RU362034}.
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DR EMBL; AP018316; BAZ87569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4V8E1; -.
DR OrthoDB; 438311at2; -.
DR Proteomes; UP000218702; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
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:RU362034};
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..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 98779 MW; 6A798CB99A55B050 CRC64;
MQPTNPNQFT EKAWEAIAHT PDVAKQYQQQ QLESEHLMKG LLEQEGLASA IFTKAGTSLQ
KVRDRTEQFI QRQPKVSGAS ASVYLGRSLD TLLDRAEKYR QEFKDEFISI EHLLLGYAKD
DRFGKSLLQE FGLDENKLKN IIKEIRGKQK VTDQNPEGKY QSLEKYGRDL TEAARKGQLD
PVIGRDDEIR RTVQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIVAGDV PQSLKDRKLI
SLDMGALIAG AKFRGEFEER LKAVLKEVTE SGGNIVLFID EIHTVVGAGA SQGAMDAGNL
LKPMLARGEL RCIGATTLDE YRKYLEKDAA LERRFQQVYV DQPNVQDTIS ILRGLKERYE
VHHGVRISDS SLVAAATLSN RYISDRFLPD KAIDLVDEAA ARLKMEITSK PEELDEIDRK
ILQLEMEKLS LQKESDLASR ERLERLEKEL ADLKEDQRTL STQWQSEKGI ITKIQSIKEE
IDRVNLEIQQ TERNYDLNRA AELKYGKLTD LHRQLQAVET ELSQTQKTGK SLLREEVTEA
DIAEIISKWT GIPLNKLVES EKEKLLHLED ELHHRVIGQQ EAVTAVADAI QRSRAGLSDP
NRPIASFVFL GPTGVGKTEL AKALAAYMFD TEEALVRIDM SEYMDKHNVS RLIGAPPGYV
GYEEGGQLTE AIRRRPYAVI LFDEIEKAHP DVFNIFLQIL DDGRVTDAQG RTVDFKNSII
IMTSNIGSQY ILDISGDDSR YDEMRNRVME AMRNSFRPEF LNRLDELIIF HSLQKSELRN
IVQLQVDRLR QRLTDRKMSL KLSSSALDFL AEVGYDPVFG ARPLKRAIQR ELETQIAKAI
LRGDFSDGDT IFVDVQNERL SFNRLPAEVF TG
//
