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Database: UniProt
Entry: K9XRA3_STAC7
LinkDB: K9XRA3_STAC7
Original site: K9XRA3_STAC7 
ID   K9XRA3_STAC7            Unreviewed;       871 AA.
AC   K9XRA3;
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=Sta7437_1578 {ECO:0000313|EMBL:AFZ35145.1};
OS   Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC   Stanieria.
OX   NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ35145.1, ECO:0000313|Proteomes:UP000010473};
RN   [1] {ECO:0000313|Proteomes:UP000010473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
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; CP003653; AFZ35145.1; -; Genomic_DNA.
DR   RefSeq; WP_015192816.1; NC_019748.1.
DR   AlphaFoldDB; K9XRA3; -.
DR   STRING; 111780.Sta7437_1578; -.
DR   KEGG; scs:Sta7437_1578; -.
DR   PATRIC; fig|111780.3.peg.1644; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_3; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000010473; 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:UP000010473};
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"
FT   COILED          779..806
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  99374 MW;  9AE32EECF3570548 CRC64;
     MQPTNPQKFT EKAWQAIVRT PDIAKENKHQ QIESEHLLKA LIEEEGLANS IFNKANISVQ
     RVRDKTDEFI NRQPKVSNLG ESVYLGRSLD TLLDRAENHR KEFGDEYISI EHLLLAYAKD
     DRLGRKLFQE FGLSENKLRE IIQDVRGSQK VTDQNPEGKY QSLEKYGREL TQLARQGKLD
     PVIGRDEEIR RTIQILSRRT KNNPVLIGEP GVGKTAIVEG LAQRIVNRDV PESLRDRKLI
     ALDMGALIAG AKYRGEFEER LKAVLKEVTE SEGNIIMFID EIHTVVGAGA TQGAMDAGNL
     LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQSVLV DEPNVIDTIS ILRGLKERYE
     VHHGVKISDT SLVAAATLSN RYISDRFLPD KAIDLVDEAA AKLKMEITSK PEELDEIDRK
     ILQLEMERLS LQKEDDILSR ERLEKLEKEL ANLKEEQSEL NAQWQSEKEV IDQIRTLKEE
     IDRVNLEIQQ AERDYDLNRA AELRYGKLTD LQRQIREIES KLAERQTTGR NMLREEVTEA
     DIAEIISKWT GIPISKLVES EKEKLLHLED ELHQRVIGQD EAVIAVADAI QRSRAGLADP
     ERPTASFIFL GPTGVGKTEL AKALAVTLFD SEEALVRIDM SEYMEKHTVS RLIGAPPGYV
     GYEEGGQLTE AIRRRPYSVI LFDEIEKAHN DVFNIMLQIL DDGRLTDSQG RTVDFKNTII
     IMTSNIGSQY ILDVAGDDNR YEEMRSRVMD AMRNNFRPEF LNRIDEIIIF HGLQKAQLRN
     IVKIQIKRLE DRLDEQKLSL KMSEAALDFL AELGYDPVYG ARPLKRAIQR YLETAIAKSI
     LRGEFKGGDT IFVDVEDERL SLKRVPVEML A
//
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