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Database: UniProt
Entry: K9Z4D2_CYAAP
LinkDB: K9Z4D2_CYAAP
Original site: K9Z4D2_CYAAP 
ID   K9Z4D2_CYAAP            Unreviewed;       873 AA.
AC   K9Z4D2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Cyan10605_1101 {ECO:0000313|EMBL:AFZ53223.1};
OS   Cyanobacterium aponinum (strain PCC 10605).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Cyanobacterium.
OX   NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ53223.1, ECO:0000313|Proteomes:UP000010480};
RN   [1] {ECO:0000313|Proteomes:UP000010480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(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; CP003947; AFZ53223.1; -; Genomic_DNA.
DR   RefSeq; WP_015218954.1; NC_019776.1.
DR   AlphaFoldDB; K9Z4D2; -.
DR   STRING; 755178.Cyan10605_1101; -.
DR   KEGG; can:Cyan10605_1101; -.
DR   PATRIC; fig|755178.3.peg.1164; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_3; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000010480; 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:UP000010480};
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   873 AA;  99025 MW;  6DFBB04FD1B3A4E5 CRC64;
     MQPTNPQQFT EKAWEAIVKT PDIAKQSQHQ QIESEHLLKS LLEQQGLATS IFNKADISLT
     RLRDRTDEFI NRQPKVKNVS DSVYLGKSLD TLLDRAEKYR KEFEDDFISI EHIILGYAQD
     ERFGKNLLRE FNLDENQLKT IIKEIRGSQK VTDQNPEGKY ESLTKYGRDL TELARQGKLD
     PVIGRDDEVR RTIQILSRRT KNNPVLIGEP GVGKTAIVEG LAQRIINRDV PESLLDRTLI
     ALDMGALIAG AKYRGEFEER LKAVLKEVTE SEGNIILFID EIHTVVGAGA TQGAMDAGNL
     LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQSVYV GEPNVIDTIS ILRGLKERYE
     VHHGVKIADN ALVAAAMLSN RYITDRFLPD KAIDLVDESA AKLKMEITSK PEELDEVDRK
     ILQLEMERLS LKKEDDPASK ERLAKLEQEL GNLKEQQSAF NAQWQSEKDI IDEIRNLRES
     IERVNVEIQQ AERDYDYNKA AELRYGKLND LQQQIKDKET ALAEKQTTGK SLLREEVEES
     DIAEIISKWT GIPISKLVES EKEKLLHLES QLHERVIGQD EAVIAVSEAI QRSRAGLSDP
     NRPTASFIFL GPTGVGKTEL AKALAGILFD TEEAIVRIDM SEYMEKHTVS RLMGAPPGYV
     GYEEGGQLTE AIRRRPYSVV LFDEIEKAHP DVFNVMLQIL DDGRLTDSQG RTVDFSNTII
     IMTSNIGSQF ILDVSGDDSK YEQMRSRVMD AMRANFRPEF LNRIDEIIIF HSLEKSQLRH
     IVKLQVARLE TRLAEQKLSL SLSESALDFL AEIGYDPVYG ARPLKRAVQK YLETAIAKSI
     LKGEFKDGDT IFVDVEDERL SLKRLPDDLL IKS
//
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