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
//