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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//