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Database: UniProt
Entry: A0A073CEF3_PLAAG
LinkDB: A0A073CEF3_PLAAG
Original site: A0A073CEF3_PLAAG 
ID   A0A073CEF3_PLAAG        Unreviewed;       874 AA.
AC   A0A073CEF3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=A19Y_1679 {ECO:0000313|EMBL:KEI66689.1};
OS   Planktothrix agardhii NIVA-CYA 126/8.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Planktothrix.
OX   NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI66689.1, ECO:0000313|Proteomes:UP000027395};
RN   [1] {ECO:0000313|EMBL:KEI66689.1, ECO:0000313|Proteomes:UP000027395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI66689.1,
RC   ECO:0000313|Proteomes:UP000027395};
RX   PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA   Christiansen G., Goesmann A., Kurmayer R.;
RT   "Elucidation of insertion elements encoded on plasmids and in vitro
RT   construction of shuttle vectors from the toxic cyanobacterium
RT   Planktothrix.";
RL   Appl. Environ. Microbiol. 80:4887-4897(2014).
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; CM002803; KEI66689.1; -; Genomic_DNA.
DR   RefSeq; WP_042153569.1; NZ_CM002803.1.
DR   AlphaFoldDB; A0A073CEF3; -.
DR   STRING; 388467.A19Y_1679; -.
DR   GeneID; 77289788; -.
DR   PATRIC; fig|388467.6.peg.1622; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_3; -.
DR   Proteomes; UP000027395; 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   Reference proteome {ECO:0000313|Proteomes:UP000027395};
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          414..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   874 AA;  98959 MW;  1983CDDD87AA0677 CRC64;
     MQPTDPNKFT EKTWEALART PDLVKQSQQQ QIETEHLMKA LLEQEGLTKN ILSKAGISVG
     QFREKTDSFI NRQPKITGTI ANVYLGRSLD TLLDKAEAYR QEYKDEFISV EHLFLAYPKD
     DRFGKALFQE FHLDETKLKS IITQIRGNNK VTDQTPENKY ESLEKYGRDL TEAARQGKLD
     PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIIAGDV PQSLQERRLI
     ALDMGALIAG AKFRGEFEER LKAVLKEVTD SNGAIILFID EIHTVVGAGA TQGAMDAGNL
     LKPMLARGEL RCIGATTLDE YRKYLEKDPA LERRFQQVYV DQPTVEDTIS ILRGLKERYE
     VHHGVKISDS ALVAAAVLST RYISDRFLPD KAIDLVDESA AKLKMEITSK PEQLDEIDRR
     ILQLEMERLS LKKESDAASL ERLERIETEL GTLKQEQQSL SSQWQSEKNV ITDIQSIKEE
     IDRVNIEIQQ AERNYDLNRA AELKYGKMEE LKKKLKAIEA QLENTQISGK TLLREEVTEA
     DIAEIISKWT GIPISKLVES EMQKLLTLED ELHHRVIGQD EAVTAVADAI QRSRAGLSDP
     NRPVASFIFL GPTGVGKTEL AKALASYLFD TEEAMVRIDM SEYMEKHAVS RLIGAPPGYV
     GYDEGGQLTE AIRRRPYTVI LFDEIEKAHP DVFNIMLQIL DDGRVTDAQG HTVDFKNSII
     IMTSNVGSQY ILDVSGSDSQ YEEMRSRVLE AMRASFRPEF LNRIDEMIIF HALQKSELRQ
     IVSLQVERLS KRLVERKMTL KLSDSALDFL AEVGYDPVYG ARPLKRAIQR ELETPIAKAI
     LRSEFVNGDT IFVDIENERL VFKRLPLELL TVQE
//
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