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Database: UniProt
Entry: A0ZE17_NODSP
LinkDB: A0ZE17_NODSP
Original site: A0ZE17_NODSP 
ID   A0ZE17_NODSP            Unreviewed;       884 AA.
AC   A0ZE17;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=NSP_3930 {ECO:0000313|EMBL:AHJ26744.1};
OS   Nodularia spumigena CCY9414.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Nodularia.
OX   NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ26744.1, ECO:0000313|Proteomes:UP000019325};
RN   [1] {ECO:0000313|EMBL:AHJ26744.1, ECO:0000313|Proteomes:UP000019325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ26744.1};
RX   PubMed=23555932;
RA   Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA   Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA   Stal L.J., Hess W.R.;
RT   "Insights into the physiology and ecology of the brackish-water-adapted
RT   Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT   analysis.";
RL   PLoS ONE 8:E60224-E60224(2013).
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}.
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DR   EMBL; CP007203; AHJ26744.1; -; Genomic_DNA.
DR   RefSeq; WP_006195814.1; NZ_CP007203.1.
DR   AlphaFoldDB; A0ZE17; -.
DR   STRING; 313624.NSP_3930; -.
DR   PATRIC; fig|313624.11.peg.392; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_3; -.
DR   Proteomes; UP000019325; 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; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          6..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          446..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   884 AA;  99586 MW;  3582C372AD449A1D CRC64;
     MQPTDPNKFT DTAWEAIVKS QDIVRAYQQQ QLDVEHLIIA LLQEPTSLAI RIFARAEVDP
     IRLQQQLEAF TQRQPKVGKS DQLYLGRNLD MLLDKADEVK VRMQDAYISV EHIILAFAED
     ERIGRRILKA FNADSAKLEA NIKTVRGSQK VTDQNPESRY EALQKFGRDL TEQAKAGKLD
     PVIGRDDEIR RVIQVLSRRS KNNPVLIGEP GVGKTAIAEA LAQRMVNGDV PESLKNRQLI
     SLDIGSLIAG AKLRGEFEER LKAVLREVTE SNGQIVLFID ELHTVVGTGS SQQGAMDAGN
     LLKPMLARGE LRCIGATTLD EYRKHIEKDA ALERRFQQVF VDQPSVENTI SILRGLKERY
     EVHHNVKISD SALVAAATLS ARYIADRFLP DKAIDLVDEA AAQLKMEITS KPAELETIDR
     RLMQLEMEKL SLAGEEKETA PARERFERIE AEIATLTVKQ QEFNEQWQGE KRLLEAISTL
     KKEEDALRVQ IEQAERAYDL NKAAQLKYGK LEGVQRDREA KEAQLLEIQN QGSTLLREQV
     IESDIAEIVA KWTGIPVNRL LASERQKLLQ LETHLHQRVI GQHEAVAAVS AAIRRARAGM
     KDPGRPIGSF LFMGPTGVGK TELARALAQF LFDSDDALIR LDMSEYMEKH SVSRLVGAPP
     GYVGYEEGGQ LSQAVRRHPY SVVLFDEVEK AHPDVFNILL QVLDDGRITD SQGRAVDFRN
     TVIVMTSNIG SEYILDVSGD DTKYEKMQTR VTDSLRSHFR PEFLNRVDDI IIFHALSRTE
     MRHIIRIQLK RVEKLLRDQK ISFEISAAAC DYLVEAGYDP VYGARPLKRA IQREVENPLA
     TKLLENTFIP GDTIFIEKEE QGLTFSKTMP VKVTVSPSSV KVLE
//
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